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Discovery of tRNA Zamecnik and Hoagland discovered a molecule that is essential for protein synthesis: tRNA. Using the cell-free system, they noticed that the RNA in a particular cytoplasmic fraction became labeled with 14C-amino acids and that the labeled RNA was subsequently able to transfer the amino acids to microsomal protein [1]. Using this system, he, Elizabeth Keller, and Mahlon Hoagland demonstrated the initial step in protein synthesis: the activation of amino acids by formation of aminoacyl adenylates from amino acids and ATP [2]. The transfer was dependent upon guanosine triphosphate. From this they concluded that the RNA, later named transfer RNA or tRNA, functions as an intermediate carrier of amino acids in protein synthesis. Zamecnik and Hoagland later contributed to our understanding of how the transfer process works. The existence of tRNA was first hypothesized by  HYPERLINK "http://en.wikipedia.org/wiki/Francis_Crick"Francis Crick, based on the assumption that there must exist an adapter molecule capable of mediating the translation of the RNA alphabet into the protein alphabet. Significant research on structure was conducted in the early 1960s by  HYPERLINK "http://en.wikipedia.org/wiki/Alex_Rich"Alex Rich and  HYPERLINK "http://en.wikipedia.org/w/index.php?title=Don_Caspar&action=edit&redlink=1"Don Caspar, two researchers in Boston, the  HYPERLINK "http://en.wikipedia.org/w/index.php?title=Jacques_Fresco&action=edit&redlink=1"Jacques Fresco group in  HYPERLINK "http://en.wikipedia.org/wiki/Princeton_University"Princeton University and a  HYPERLINK "http://en.wikipedia.org/wiki/United_Kingdom"United Kingdom group at  HYPERLINK "http://en.wikipedia.org/wiki/King's_College_London"King's College London.[3] What is tRNA tRNA or Transfer Ribonucleic Acid is the information adapter molecule and aminoacyl-tRNA synthetases (AARS) are the very special enzymes that attach the correct amino acid to each tRNA.. It is the direct interface between amino-acid sequence of a protein and the information in DNA. Therefore it decodes the information in DNA. There are 20 different tRNA molecules. All have between 75-95 nt.All tRNA's from all organisms have a similar structure, indeed a human tRNA can function in yeast cells. tRNA transfers a specific  HYPERLINK "http://en.wikipedia.org/wiki/Amino_acid"amino acid to a growing polypeptide chain at the ribosomal site of protein synthesis during  HYPERLINK "http://en.wikipedia.org/wiki/Translation_(biology)"translation. It has a  HYPERLINK "http://en.wikipedia.org/wiki/Directionality_(molecular_biology)"3' terminal site for amino acid attachment. This covalent linkage is catalyzed by an  HYPERLINK "http://en.wikipedia.org/wiki/Aminoacyl_tRNA_synthetase"aminoacyl tRNA synthetase. It also contains a three  HYPERLINK "http://en.wikipedia.org/wiki/Nucleotide"base region called the  HYPERLINK "http://en.wikipedia.org/wiki/Anticodon"anticodon that can base pair to the corresponding three base  HYPERLINK "http://en.wikipedia.org/wiki/Codon"codon region on  HYPERLINK "http://en.wikipedia.org/wiki/MRNA"mRNA. Each type of tRNA molecule can be attached to only one type of amino acid, but because the  HYPERLINK "http://en.wikipedia.org/wiki/Genetic_code"genetic code contains multiple codons that specify the same amino acid, tRNA molecules bearing different anticodons may also carry the same amino acid. tRNA is synthesized in two parts. The body of the tRNA is transcribed from a tRNA gene. The acceptor stem is the same for all tRNA molecules and is added after the body is synthesized. It is replaced often during lifetime of a tRNA molecule.Transfer RNA is the "adaptor" molecule hypothesized by  HYPERLINK "http://en.wikipedia.org/wiki/Francis_Crick"Francis Crick, which mediates recognition of the  HYPERLINK "http://en.wikipedia.org/wiki/Codon"codon sequence in  HYPERLINK "http://en.wikipedia.org/wiki/MRNA"mRNA and allows its translation into the appropriate amino acid. Binding to Ribosome The ribosome has three binding sites for tRNA molecules: the A, P and E sites. During translation the A site binds an incoming aminoacyl-tRNA as directed by the codon currently occupying this site. This codon specifies the next amino acid to be added to the growing peptide chain. The A site is only working after the first aminoacyl-tRNA has attached to the P site. The P-site codon is occupied by peptdyl-tRNA that is a tRNA with multiple amino acids attached as a long chain. The P site is actually the first to bind to aminoacyl tRNA. This tRNA in the P site carries the chain of amino acids that has already been synthesized. The E site is occupied by the empty tRNA as it is about to exit the ribosome. Structure of tRNA Transfer RNA is a fairly small molecule, consisting of 75-90 nucleotides, which folds over itself (via hydrogen bonding between base pairs at four different sites), forming a three-dimensional L-shaped structure. The double stranded sites are referred to as stems and the non-bonded sites as loops. PRIMARY AND SECONDARY STRUCTURES Clover leaf structure of tRNA (a) Acceptor arm: In the tRNA, the acceptor stem is made up of seven base pairs (1-7, 66-76). The acceptor stem may contain non-Watson-Crick base pairs.At the 3' end of the acceptor stem is the amino acid attachment site (74-76). This is where the synthetase molecule activates the tRNA by attaching serine. The acceptor stem is believed to carry the primary identity elements for recognition. The amino acid is bound to the CCA sequence at the 3' end of the tRNA. This sequence is important for the recognition of tRNA by enzymes critical in translation. In prokaryotes, the CCA sequence is transcribed. In eukaryotes, the CCA sequence is added during processing and therefore does not appear in the tRNA gene. (b) T-arm: The T-arm consists of a T-stem (five base pairs; 49-53, 61-65) and T-loop (55-60). This arm contains the conserved sequence of the three ribonucleotides, ribothymidine, pseudouridine and cytosine. p is so named because it contains thymine , a nucleotide that is found in DNA but not in any other RNA species besides tRNA. The T-loop is an important region serving as a recognition site for the ribosome. Base number 57 is always a purine, while 59 and 60 are pyrimidines    !"#$%&'()*+,-./0123456789:;<=>?@ABCDEFGHIJKLMNOPQRSTUVWXYZ[\]^_`abcdefghijklmnopqrstuvwxyz{|}~      !"#$%&'()*+,-./0123456789:;<=>?@ABCDEFGHIJKLMNOPQRSTUVWXYZ[\]^_`abcdefghijklmnopqrstuvwxyz{|}~      !"#$%&'()*+,-./0123456789:;<=>?@ABCDEFGHIJKLMNOPQRSTUVWXYZ[\]^_`abcdefghijklmnopqrstuvwxyz{|}~      !"#$%&'()*+,-./0123456789:;<=>?@ABCDEFGHIJKLMNOPQRSTUVWXYZ[\]^_`abcdefghijklmnopqrstuvwxyz{|}~      !"#$%&'()*+,-./0123456789:;<=>?@ABCDEFGHIJKLMNOPQRSTUVWXYZ[\]^_`abcdefghijklmnopqrstuvwxyz{|}~ in most cases [4]. (c) Anticodon arm: The anticodon arm is comprised of the anticodon stem (five base pairs; 27-31, 39-43) and its corresponding loop region (32-38). The anticodon region itself includes nucleotides 34, 35, 36. An anticodon[5] is a unit made up of three  HYPERLINK "http://en.wikipedia.org/wiki/Nucleotides"nucleotides that correspond to the three bases of the codon on the mRNA. Each tRNA contains specific anticodon triplet sequences that can base-pair to one or more codons for an amino acid. (d) D-arm: The D-arm is made up of the D-stem (four base pairs; 10-13, 22-25) and the D-loop (14-21). This region is so named because it contains the modified base dihydrouracil. The D-stem is also believed to contain some identity elements for recognition. A major feature of the D-loop is a "zig-zag" conformation of the backbone, specifically caused by a bulging in of the G20 residue. The D-loop is a highly variable region and in some cases is thought to be an important recognition site for the enzyme that will attach the amino acids (aminoacyl-tRNA synthetase; transferase). Enlargement of the D-loop appears essential to maintaining astable tertiary structure in this species, while rearrangement of a base triple in the augmented D-stem is critical for efficient glutaminylation. (e) V-loop: The variable loop (44-48) protrudes at approximately a 45 degree angle to the plane of the L-shaped tRNA. Prokaryotes have three amino acid-specific class II tRNAs that possess a characteristic long variable arm, tRNASer, tRNALeuand tRNATyr, while eukaryotes have only two, tRNASerand tRNALeu. Because of such a phylogenetic divergence in the composition of tRNA, the class II tRNA system is a good candidate for studying how the tRNA recognition manner has evolved in association with the evolution of tRNA [6]. The recognition manner of class II tRNA, especially the discrimination strategy of each aminoacyl-tRNA synthetase against noncognate class II tRNAs, is significantly divergent between E.coli and yeast. This difference is thought to be due mainly to the different composition of class II tRNAs in E.coli and yeast.  Figure 2: Clover leaf structure of tRNA. The tRNA is drawn in the conventional cloverleaf structure, with the different components labeled. Invariant nucleotides (A, C, G, T, U, Y, where Y = pseudouridine) and semi-invariant nucleotides (abbreviations: R, purine; Y, pyrimidine) are indicated. Optional nucleotides not present in all tRNAs are shown as smaller dots. The standard numbering system places position 1 at the 5 end and position 76 at the 3 end; it includes some but not all of the optional nucleotides. The invariant and semi-invariant nucleotides are at positions 8, 11, 14, 15, 18, 19, 21, 24, 32, 33, 37, 48, 53, 54, 55, 56, 57, 58, 60, 61, 74, 75 and 76. The nucleotides of the anticodon are at positions 34, 35 and 36. IMPORTANCE OF 3D BASE PAIRING The 3D base pairing is very important for the stabilization of the tRNA structure and maintaining the L- shape [7,8, 9]. The tertiary structure of the DT region is of special interest and has been the subject of a number of studies [10,11,12, 13]. Analysis of the nucleotide sequences of the selected clones demonstrates that among the randomized nucleotides, the most conservative are nucleotides 54 and 58 in the T-loop. In most cases, they make the combination U54-A58, which allows the formation of the normal reverse Hoogsteen base pair. Surprisingly, other clones have either the combination G54-A58 or G54-G58. However, molecular modeling shows that these purine purine base pairs can very closely mimic the reverse Hoogsteen base pair U-A and thus can replace it in the T-loop of a functional tRNA. This places the reverse Hoogsteen base pair 54-58 as one of the most important structural aspects of tRNA functionality. The major role of this base pair is to preserve the conformation of dinucleotide 59 60 and, through this, to maintain the general architecture of the tRNA L-form as stated before [14]. Importance of Nucleotide-33 In bacteria such as E.coli the nucleotide 33 is of great importance. In E. coli a UGA codon can be efficiently suppressed by a suppressor tRNA (Trp) called Su9 [15,16,17,18, 19]. It has been seen that the level of UGA suppression is determined by the nature of the nucleotide at the 5' side of the anticodon of the suppressor (position 33). UGA suppression occurs when a pyrimidine residue is located in position 33 of the tRNA, and suppression is more efficient with a U than with a C in this position. On the other hand, when a purine residue is located at this position UGA suppression is extremely low. These results show that in the case of tRNA Su9, the UGA codon context effect does not require base pairing between the nucleotide at the 3' side of the codon and the 5' side of the anticodon [20]. Importance of Nucleotide-47 It has been seen that the vast majority of cytoplasmic tRNAs that lack nt 47 contain a wobble U13:G22 base pair, even though this base pair is overwhelmingly populated by C13:G22 in tRNAs with nt 47.Notably, all exceptions to this correlation are tRNAGly, some of which are known not to promote ribosome bound protein synthesis. In order to establish a possible functional basis for the correlation observed with cytoplasmic tRNAs, tRNA genes were constructed containing either the wobble U13:G22 or theWatson Crick C13:G22 base pair, both in the absence of nt 47, to test their in vivo activity. It is seen that tRNAs lacking nt 47 with the C13:G22 base pair are actually more active in suppression of amber codons, whereas the two tRNAs have comparable activities in more normal protein synthesis. However,cells harboring tRNAs lacking nt 47 with the U13:G22 base pair outgrow cells with the C13:G22 tRNA in experiments of long-term growth incorporating significant periods of latency[21]. L Shape Tertiary Structure Of tRNA 1. Acceptor stem stacks on the TYC arm. Anticodon arm stacks on the D arm. The resulting coaxial helices are nearly normal A-form RNA [22]. 2. Most of the bases (71/76) are stacked; only about half are base paired. 3. Mg2+ bound in the "corner of the L" stabilizes the structure. 4. The tertiary structure is stabilized by base pairing and base stacking. 5. Examples of non-standard base-base interactions. a) The "wobble" base pair is present. b) Base triple interactions; a base inserts into the deep groove of a standard base pair (distant in sequence). c) Intercalation of bases at two locations. These, and several other tertiary structure motifs, have also been found in the compact, folded structures of many other RNAs [23].  Figure 3: L SHAPED TERTIARY STRUCTURE OF tRNA tRNA & AMINOACYL-tRNA SYNTHETASE Each tRNA is charged with the proper amino acid via a covalent ester bond at their 3' end by a family of enzymes called aminoacyl-tRNA synthetases. Each enzyme must recognize both the tRNA(s) specific for an amino acid and the corresponding amino acid. This energy-consuming process is ATP-dependent and results in the cleavage of two high-energy phosphate bonds (one in going from ATP to AMP + PP, and one for the cleavage of pyrophosphate into two inorganic phosphates). The accuracy of protein translation depends on the fidelity with which the correct amino acids are esterified to their cognate tRNA molecules by aminoacyl tRNA synthetases. Despite the structural differences between Class I and Class II, all aminoacyl tRNA synthetases carry out the same two-step reaction. Step 1 : In the first step, the enzyme binds ATP and the amino acid, and catalyzes the formation of an aminoacyl-adenylate intermediate, in which a covalent linkage is formed between the 5'-phosphate group of ATP and the carboxyl end of the amino acid [24,25]. The aminoacyl tRNA synthetase uses the energy generated by ATP hydrolysis to activate the amino acid, forming the aminoacyl-AMP that remains associated with the enzyme [25].The bonds between phosphate groups in ATP are high energy bonds. When they are broken, this energy is trapped in the aminoacyl-AMP, which is why we call this an activated amino acid. Step 2 In the second step, the amino acid is transferred to the appropriate tRNA and bonded covalently to either the 2'OH or 3'OH of the invariant 3' adenosine terminal of the tRNA molecule. The energy in the aminoacyl-AMP is used to transfer the amino acid to the tRNA forming amioacyl-tRNA.  FIGURE 4: Two step reaction carried out by aminoacyl tRNA synthetases Factors that determine the specificity of tRNA synthetases: Specific anticodon in tRNA Other recognition regions: the base next to the CCA in the acceptor stem correlates with the nature of the cognate amino acid of that tRNA Single base pair in acceptor stem 3D structure of tRNA synthetases There are 20 different aminoacyl-tRNA synthetases, one for each amino acid. Despite the fact that they all carry out very similar tasks, they vary greatly in size (40-100 kDalton). Accurate translation of the genetic code depends on attachment of each amino acid to an appropriate tRNA. Each aaRS recognizes its particular amino acid and tRNAs coding for that amino acid. Since there are 61 amino acid codons, most tRNA synthetases must be able to recognize more than one type of tRNA (i.e. 6 codons for Arg). These tRNAs are called cognate tRNAs for that particular synthetase. This mapping is achieved through so-called recognition domains on the tRNA.  FIGURE 5: tRNA shown with red backbone and yellow bases tRNA synthetase shown as space-filling model in blue. Domains of tRNA recognized by an aaRS are called identity elements. Most identity elements are located in the acceptor stem and anticodon loop. Aminoacyl-tRNA Synthetases arose early in evolution. Early aaRSs probably recognized tRNAs only by their acceptor stems Accuracy & Proofreading: The accuracy of charging tRNA with the proper amino acid is crucial because once charged, only the tRNA anticodon determines incorporation, not the attached amino acid. The error rate of charging is very low: 1 in 10,000. This is achieved by two means: the amino acid specificity pocket in a specific synthetase will only bind amino acids similar in size and charge. the synthetase also has proofreading capability which, once a wrong aminoacyl-adenylate complex is formed (1st step), will hydrolyze the complex before it can be covalently attached to the tRNA (2nd step). CLASSES OF AMINOACYL tRNA SYNTHETASE Aminoacyl-tRNA synthetases from all organisms belong to one of two classes depending on the amino acid they are responsible for. Class I enzymes are generally (though not always) monomeric, and attach the carboxyl of their target amino acid to the 2' OH of adenosine 76 in the tRNA molecule [26,27]. Class II enzymes are generally dimeric or tetrameric, and attach their amino acid to the 3' OH of their tRNA, except for phenylalaninyl-tRNA synthetase, which uses the 2' OH [28].  Introns: In 1977, a surprising phenomenon was discovered  introns. These are sequences of DNA, within genes, which have no apparent purpose. The genes containing them were called "split genes." Introns almost never appear within prokaryotic cells. They are rare within single-celled eukaryotes. However, within the cells of multicelled animals and plants almost every gene has introns. Introns are interruptions in the text of eukaryotic genes. Every time the genome is replicated, they are replicated right along with it. BACTERIAL INTRONS Although the intron early theory stated that bacteria had no introns, yet there have been some discoveries where bacterial introns were found. Infact the cyanobacterial tRNAleu (UAA) sequences from the databases, have been used to study the evolutionary patterns in this genetic marker and to thus gain interesting insights into its evolution [29]. The Cyanobacterial tRNALeu (UAA) Intron: Evolutionary Patterns in a Genetic Marker Since the time introns were discovered, their origin has been debated and different theories have been proposed [30,31]. Group-I and -II introns are two types of RNA enzymes that catalyze their own splicing by different mechanisms [32]. The ability of group-I introns to catalyze their own splicing is dependent on their highly conserved secondary and tertiary structures. Different group-I introns have little sequence similarity, but all share a series of short conserved elements, P, Q, R, and S, known as the catalytic core [33]. The tRNALeu (UAA) intron in cyanobacteria is a group-I intron and has been suggested to be of ancient origin because it interrupts, in all known cases, the tRNA gene at a conserved position in the anticodon triplet (between the second and third base). Moreover, the tRNALeu (UAA) introns from cyanobacteria and chloroplasts show high homology and they are more closely related to each other than to any other known sequences, indicating an early origin. The fact that the intron is not found in all, but in many cyanobacterial and chloroplast lineages is best explained by multiple losses [34,35]. However, the evolutionary history of the tRNALeu (UAA) intron is still debated, and it has been suggested that the intron is of more recent origin and has been introduced through lateral transfer [36]. In this study the evidence supporting these theories are discussed. In a number of studies, tRNALeu (UAA) intron is used as a marker for diversity and specificity of cyanobacteria symbiotically associated with plants and fungi [37,38,39,40]. The symbioses we have been interested in all contain cyanobacteria of the Nostoc type as their symbiont. The tRNALeu (UAA) intron has been instrumental in revealing both interesting patterns of diversity and spatial distribution of the cyanobacterial symbionts. Previous studies provided with a large number of sequences from closely related Nostoc strains from natural populations. Using these sequences, as well as other tRNALeu (UAA) intron sequences from the databases, it is possible to study evolutionary patterns in this genetic marker and to thus gain interesting insights into its evolution. ARCHAEAL INTRONS: Most introns of archaeal tRNA genes (tDNAs) are located in the anticodon loop, between nucleotides 37 and 38 (canonical position), the unique location of their eukaryotic counterparts. However, in several Archaea, mostly in Crenarchaeota, introns have been found at many other positions of the tDNAs [54]. These are distributed among 14 different positions within the pre-tRNA molecules: in the anticodon branch, in the variable arm, and in the D- and T-loops as well as in the amino acid arm. Among all archaea examined, the crenarchaeon P. aerophilum contains the largest number of tDNA introns (26 altogether), the largest proportion introns located at non-canonical positions. The non-canonical positions are like 32/33 of anticodon arm, 20b/21 of D-arm etc. (shown in the figure below).[41]  FIGURE 6. Intron exon sequences in selected archaeal tDNAs sorted out as a function of the type of their splicing motifs. (A) Only 30 sequences of intron exon junctions (out of a total of 103 sequences in the 800 tDNAs analyzed; see Supplementary Material) corresponding to intron located at position 37/38 are listed. The sequences shown extend from base 27 to base 43 of the anticodon arm. Uppercase letters correspond to exonic sequence and the lowercase letters to the intronic sequence. (B) The 33 sequences of intron exon junctions corresponding to introns located at positions other than 37/38. At the bottom of B is the consensus sequence of the splicing motif corresponding to the 33 sequences listed in this panel. (C) Generalized consensus from sequences shown in A and B. ARAGORN and tRNA-scan-SE In archaea and eukaryotes approximately 15% tRNA precursors contain intron(s). Although most of them are located at the unique canonical position 37 and 38 (37/38), recent report indicates that introns are also located in various non-canonical positions. TRNA-scan-SE and ARAGORN are widely used that identify tRNA genes without introns or with introns at canonical positions. A program, tRNAscan-SE [42], which identifies 99-100% of transfer RNA genes in DNA sequence while giving less than one false positive per 15 gigabases. Two previously described tRNA detection programs are used as fast, first-pass prefilters to identify candidate tRNAs, which are then analyzed by a highly selective tRNA covariance model. This work represents a practical application of RNA covariance models, which are general, probabilistic secondary structure profiles based on stochastic context-free grammars. TRNAscan-SE searches at approximately 30 000 bp/s. Additional extensions to tRNAscan-SE detect unusual tRNA homologues such as selenocysteine tRNAs, tRNA-derived repetitive elements and tRNA pseudogenes. A computer program, ARAGORN [43], identifies tRNA and tmRNA genes. The program employs heuristic algorithms to predict tRNA secondary structure, based on homology with recognized tRNA consensus sequences and ability to form a base-paired cloverleaf. tmRNA genes are identified using a modified version of the BRUCE program. ARAGORN achieves a detection sensitivity of 99% from a set of 1290 eubacterial, eukaryotic and archaeal tRNA genes and detects all complete tmRNA sequences in the tmRNA database, improving on the performance of the BRUCE program. By default, ARAGORN does not search for tRNA genes with C-loop introns, but can be configured to detect tRNA genes with C-loop introns from one to 3000 bases long. In this case, the position of the intron in the C-loop is predicted. In contrast, tRNAscan-SE has a default intron plus V-loop length of 116 bases, and there is no upper bound on intron length other than poor search speed. All introns are assumed to be situated at the same position within the C-loop. When it comes to speed, ARAGORN configured with an upper intron limit of 100 bases is more than five times faster than tRNAscan-SE in the G + C content range of 40 60%. For detection of archaeal and eubacterial tRNA genes, the results indicate that ARAGORN achieves a slightly better sensitivity than tRNAscan-SE. For eukaryotic tRNA genes, the results indicate a slightly lower sensitivity than tRNAscan-SE. ARAGORN is configured with a maximum intron size of 100 nucleotides, which roughly corresponds to the tRNAscan-SE default setting. A subset of the latest release (January 1999) of the Sprinzl compilation of tRNA gene sequences (12) is used to test the sensitivity of tRNA search algorithm. [44] AIM: We therefore developed a program FindtRNA that identifies tRNA genes without introns or with introns at canonical positions or also at non-canonical positions. The program employs algorithm to find number of tRNA present in the supplied genome sequence and predict the tRNA secondary (cloverleaf) structure of those tRNAs. We take some positions conserved to construct the tRNA coverleaf structure which are 99 % conserved according to the figure below.[45].  FIG: Canonical cloverleaf structure of tRNA, highlighting conserved positions. Positions with greater than 90% conservationare shown in black, positions with conservation between 75% and 90% are shown in dark gray, and positions with between 50% and 75% conservation are shown in light gray. The mostfrequent base across all tRNAs is shown, the conventional position number is shown as a black subscript, and the degree of conservation is shown as a gray subscript. Note that positions that are shown as dashes indicate that the most frequent state at that position is for the base to be missing (i.e., a gap). ALGORITHM: Step 1: In the first step,the whole genome sequence is reversed. Step 2: Here the numbering scheme is just opposite the picture shown above,like the 76th position is taken as 0th position,75th as 1st and so on. Step 3:A tetranucleotide sequence CTTG in the sequence which is a subset of B box consensus sequence are searched. Step 4: 20 have been deducted from the position it got for each CTTG to get the starting position of possible tRNA according to our numbering scheme. Step 5: Then the possible positions of tRNA are stored into an array. Step 6: For each position (p) the algorithm attempt to construct tRNA structure. Step 7: Then first the (p+15)th nucleotide is checked for C. If the condition is come to be true the tRNA then it attempts to construct T-loop of 7bp long and T-stem of 3-4 bp long. Else Step 8: Step 9: position (p+11)th to (p+14)th are stored in a StringBuffer tArm. Step 10:Position (p+24)th to (p+27)th are stored in another StringBuffer RevtArm. Step 11:Then the base paring are checked for 11th and 27th ,12th and 26th ,13 and 27th ,14 and 28th. Base pairing are of  HYPERLINK "http://en.wikipedia.org/wiki/Base_pair"Watson-Crick base pairs or wobble base pair. Step 7: Else it start checking for the next position(p). Step 8: After constructing T-loop and T-arm the algorithm tries to construct the Anticodon- Arm. Step 9: A for loop has encountered to deal with the V-loop and Canonical introns of total length 50. Step 10: References REFERENCE Zamecnik, P. C., and Keller, E. B. (1954) Relation between phosphate energy donors and incorporation of labeled amino acids into proteins. J. Biol. Chem. 209, 337 354 Hoagland, M. B., Keller, E. B., and Zamecnik, P. C. (1956) Enzymatic carboxyl activation of amino acids. J. Biol. Chem. 218, 345 358 Brian F.C. Clark (October 2006). " HYPERLINK "http://www.ias.ac.in/jbiosci/clark3176.pdf"The crystal structure of tRNA". J. Biosci. 31 (4): 453-7.  HYPERLINK "http://www.ncbi.nlm.nih.gov/pubmed/17206065"PMID 17206065 Sprinzl, M., Horn,C., Brown,M., Ioudovitch,A. and Steinberg,S. (1998) Compilation of tRNA sequences and sequences of tRNA genes. NucleicAcids Res., 26, 148-153 Felsenfeld G, Cantoni G. 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Lindblad, (1998), Cyanobiont specificity in some Nostoc-containing lichens and in a Peltigera aphthosa photosymbiodeme, New Phytol, 139,517-524 Costa J.-L., P. Paulsrud, P. Lindblad, (1999), Cyanobiont diversity within coralloid roots of selected cycad species, FEMS Microbiol. Ecol, 28,85-91 Hartweel, Leland; Leroy Hodd; Michael Goldberg; Ann Reynolds; Lee Silver; and Ruth Veres. Genetics: From Genes to Genomes. Boston: Mgraw-Hill, 1999. Biou et al. (1994) Structure of ser-tRNA synthetase - tRNA complex, Science 263, 1404-1410. TRNAscan-SE: a program for improved detection of transfer RNA genes in genomic sequence.  HYPERLINK "http://www.ncbi.nlm.nih.gov/sites/entrez?Db=pubmed&Cmd=Search&Term="Lowe TM,  HYPERLINK "http://www.ncbi.nlm.nih.gov/sites/entrez?Db=pubmed&Cmd=Search&Term="Eddy SR  HYPERLINK "javascript:AL_get(this, 'jour', 'Nucleic Acids Res.');"Nucleic Acids Res. 1997 Mar 1; 25(5):955-64. ARAGORN, a program to detect tRNA genes and tmRNA genes in nucleotide sequences.Dean Laslett and Bjorn Canback Nucleic Acids Res. 2004; 32(1): 11 16. Published online 2004 January 2. doi: 10.1093/nar/gkh152. 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