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J Bacteriol. 1994 February; 176(3): 547–552.
PMCID: PMC205089

Initiator transfer RNAs.

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Selected References

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  • Atherly AG, Menninger JR. Mutant E. coli strain with temperature sensitive peptidyl-transfer RNA hydrolase. Nat New Biol. 1972 Dec 20;240(103):245–246. [PubMed]
  • Chattapadhyay R, Pelka H, Schulman LH. Initiation of in vivo protein synthesis with non-methionine amino acids. Biochemistry. 1990 May 8;29(18):4263–4268. [PubMed]
  • Dickerman HW, Steers E, Jr, Redfield BG, Weissbach H. Methionyl soluble ribonucleic acid transformylase. I. Purification and partial characterization. J Biol Chem. 1967 Apr 10;242(7):1522–1525. [PubMed]
  • Dube SK, Marcker KA, Clark BF, Cory S. Nucleotide sequence of N-formyl-methionyl-transfer RNA. Nature. 1968 Apr 20;218(5138):232–233. [PubMed]
  • Dutka S, Meinnel T, Lazennec C, Mechulam Y, Blanquet S. Role of the 1-72 base pair in tRNAs for the activity of Escherichia coli peptidyl-tRNA hydrolase. Nucleic Acids Res. 1993 Aug 25;21(17):4025–4030. [PMC free article] [PubMed]
  • Gold L. Posttranscriptional regulatory mechanisms in Escherichia coli. Annu Rev Biochem. 1988;57:199–233. [PubMed]
  • Gualerzi CO, Pon CL. Initiation of mRNA translation in prokaryotes. Biochemistry. 1990 Jun 26;29(25):5881–5889. [PubMed]
  • Guillon JM, Mechulam Y, Schmitter JM, Blanquet S, Fayat G. Disruption of the gene for Met-tRNA(fMet) formyltransferase severely impairs growth of Escherichia coli. J Bacteriol. 1992 Jul;174(13):4294–4301. [PMC free article] [PubMed]
  • Guillon JM, Mechulam Y, Blanquet S, Fayat G. Importance of formylability and anticodon stem sequence to give a tRNA(Met) an initiator identity in Escherichia coli. J Bacteriol. 1993 Jul;175(14):4507–4514. [PMC free article] [PubMed]
  • Guillon JM, Meinnel T, Mechulam Y, Lazennec C, Blanquet S, Fayat G. Nucleotides of tRNA governing the specificity of Escherichia coli methionyl-tRNA(fMet) formyltransferase. J Mol Biol. 1992 Mar 20;224(2):359–367. [PubMed]
  • Hartz D, Binkley J, Hollingsworth T, Gold L. Domains of initiator tRNA and initiation codon crucial for initiator tRNA selection by Escherichia coli IF3. Genes Dev. 1990 Oct;4(10):1790–1800. [PubMed]
  • Ishii S, Kuroki K, Imamoto F. tRNAMetf2 gene in the leader region of the nusA operon in Escherichia coli. Proc Natl Acad Sci U S A. 1984 Jan;81(2):409–413. [PubMed]
  • Kössel H, RajBhandary UL. Studies on polynucleotides. LXXXVI. Enzymic hydrolysis of N-acylaminoacyl-transfer RNA. J Mol Biol. 1968 Aug 14;35(3):539–560. [PubMed]
  • Kozak M. Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles. Microbiol Rev. 1983 Mar;47(1):1–45. [PMC free article] [PubMed]
  • Laalami S, Putzer H, Plumbridge JA, Grunberg-Manago M. A severely truncated form of translational initiation factor 2 supports growth of Escherichia coli. J Mol Biol. 1991 Jul 20;220(2):335–349. [PubMed]
  • Lee CP, Dyson MR, Mandal N, Varshney U, Bahramian B, RajBhandary UL. Striking effects of coupling mutations in the acceptor stem on recognition of tRNAs by Escherichia coli Met-tRNA synthetase and Met-tRNA transformylase. Proc Natl Acad Sci U S A. 1992 Oct 1;89(19):9262–9266. [PubMed]
  • Lee CP, Mandal N, Dyson MR, RajBhandary UL. The discriminator base influences tRNA structure at the end of the acceptor stem and possibly its interaction with proteins. Proc Natl Acad Sci U S A. 1993 Aug 1;90(15):7149–7152. [PubMed]
  • Lee CP, RajBhandary UL. Mutants of Escherichia coli initiator tRNA that suppress amber codons in Saccharomyces cerevisiae and are aminoacylated with tyrosine by yeast extracts. Proc Natl Acad Sci U S A. 1991 Dec 15;88(24):11378–11382. [PubMed]
  • Lee CP, Seong BL, RajBhandary UL. Structural and sequence elements important for recognition of Escherichia coli formylmethionine tRNA by methionyl-tRNA transformylase are clustered in the acceptor stem. J Biol Chem. 1991 Sep 25;266(27):18012–18017. [PubMed]
  • Mandal N, RajBhandary UL. Escherichia coli B lacks one of the two initiator tRNA species present in E. coli K-12. J Bacteriol. 1992 Dec;174(23):7827–7830. [PMC free article] [PubMed]
  • Ono Y, Skoultchi A, Klein A, Lengyel P. Peptide chain elongation: discrimination against the initiator transfer RNA by microbial amino-acid polymerization factors. Nature. 1968 Dec 28;220(5174):1304–1307. [PubMed]
  • Rich A, RajBhandary UL. Transfer RNA: molecular structure, sequence, and properties. Annu Rev Biochem. 1976;45:805–860. [PubMed]
  • Schulman LH. Recognition of tRNAs by aminoacyl-tRNA synthetases. Prog Nucleic Acid Res Mol Biol. 1991;41:23–87. [PubMed]
  • Schulman LH, Pelka H. The structural basis for the resistance of Escherichia coli formylmethionyl transfer ribonucleic acid to cleavage by Escherichia coli peptidyl transfer ribonucleic acid hydrolase. J Biol Chem. 1975 Jan 25;250(2):542–547. [PubMed]
  • Schulman LH, Pelka H. In vitro conversion of a methionine to a glutamine-acceptor tRNA. Biochemistry. 1985 Dec 3;24(25):7309–7314. [PubMed]
  • Seong BL, Lee CP, RajBhandary UL. Suppression of amber codons in vivo as evidence that mutants derived from Escherichia coli initiator tRNA can act at the step of elongation in protein synthesis. J Biol Chem. 1989 Apr 15;264(11):6504–6508. [PubMed]
  • Seong BL, RajBhandary UL. Escherichia coli formylmethionine tRNA: mutations in GGGCCC sequence conserved in anticodon stem of initiator tRNAs affect initiation of protein synthesis and conformation of anticodon loop. Proc Natl Acad Sci U S A. 1987 Jan;84(2):334–338. [PubMed]
  • Seong BL, RajBhandary UL. Mutants of Escherichia coli formylmethionine tRNA: a single base change enables initiator tRNA to act as an elongator in vitro. Proc Natl Acad Sci U S A. 1987 Dec;84(24):8859–8863. [PubMed]
  • Sundari RM, Stringer EA, Schulman LH, Maitra U. Interaction of bacterial initiation factor 2 with initiator tRNA. J Biol Chem. 1976 Jun 10;251(11):3338–3345. [PubMed]
  • Varshney U, Lee CP, RajBhandary UL. Direct analysis of aminoacylation levels of tRNAs in vivo. Application to studying recognition of Escherichia coli initiator tRNA mutants by glutaminyl-tRNA synthetase. J Biol Chem. 1991 Dec 25;266(36):24712–24718. [PubMed]
  • Varshney U, Lee CP, RajBhandary UL. From elongator tRNA to initiator tRNA. Proc Natl Acad Sci U S A. 1993 Mar 15;90(6):2305–2309. [PubMed]
  • Varshney U, Lee CP, Seong BL, RajBhandary UL. Mutants of initiator tRNA that function both as initiators and elongators. J Biol Chem. 1991 Sep 25;266(27):18018–18024. [PubMed]
  • Varshney U, RajBhandary UL. Initiation of protein synthesis from a termination codon. Proc Natl Acad Sci U S A. 1990 Feb;87(4):1586–1590. [PubMed]
  • Varshney U, RajBhandary UL. Role of methionine and formylation of initiator tRNA in initiation of protein synthesis in Escherichia coli. J Bacteriol. 1992 Dec;174(23):7819–7826. [PMC free article] [PubMed]
  • Wagner T, Gross M, Sigler PB. Isoleucyl initiator tRNA does not initiate eucaryotic protein synthesis. J Biol Chem. 1984 Apr 25;259(8):4706–4709. [PubMed]
  • Wakao H, Romby P, Westhof E, Laalami S, Grunberg-Manago M, Ebel JP, Ehresmann C, Ehresmann B. The solution structure of the Escherichia coli initiator tRNA and its interactions with initiation factor 2 and the ribosomal 30 S subunit. J Biol Chem. 1989 Dec 5;264(34):20363–20371. [PubMed]
  • Woo NH, Roe BA, Rich A. Three-dimensional structure of Escherichia coli initiator tRNAfMet. Nature. 1980 Jul 24;286(5771):346–351. [PubMed]
  • Wrede P, Woo NH, Rich A. Initiator tRNAs have a unique anticodon loop conformation. Proc Natl Acad Sci U S A. 1979 Jul;76(7):3289–3293. [PubMed]

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