HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Mangroo, D. Articles by RajBhandary, U. L. Search for Related Content PubMed PubMed Citation Articles by Mangroo, D. Articles by RajBhandary, U. L. Social Bookmarking                      What's this?

Volume 270, Number 20, Issue of May 19, pp. 12203-12209, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.

---

Dev Mangroo , Uttam L. RajBhandary

We describe the effects of overproduction of methionyl-tRNA transformylase and initiation factors IF2 and IF3 on the activity, in vivo, of initiator tRNA mutants defective at specific steps of the initiation process in protein synthesis. The activity of the U35A36/G72 and U35A36/G72G73 mutants, which are defective in formylation, was increased by overproduction of methionyl-tRNA transformylase. In contrast, the activity of the C30:G40/U35A36 mutant, which is formylated normally but is defective in binding to the ribosomal P site, was not increased. Overproduction of IF2 had a strong stimulatory effect on the activity of virtually all the mutants carrying the U35A36 anticodon sequence change, including the U35A36, U35A36/G72, U35A36/G72G73, and the C30:G40/U35A36 mutants. In cells overproducing IF2, the amount of protein made by translation of a mutant mRNA, which uses the U35A36 mutant initiator tRNA, is severalfold higher than that made by translation of a wild type mRNA. We discuss the possible implications of this result on overproduction of proteins and on the order of assembly of the 30 S ribosome mRNA fMet-tRNA initiation complex in Escherichia coli. Overproduction of IF3 did not affect the initiator activity of any of the tRNA mutants studied.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				N. S. Singh, G. Das, A. Seshadri, R. Sangeetha, and U. Varshney Evidence for a role of initiation factor 3 in recycling of ribosomal complexes stalled on mRNAs in Escherichia coli Nucleic Acids Res., September 30, 2005; 33(17): 5591 - 5601. [Abstract] [Full Text] [PDF]

				G. Das, T. K. Dineshkumar, S. Thanedar, and U. Varshney Acquisition of a stable mutation in metY allows efficient initiation from an amber codon in Escherichia coli Microbiology, June 1, 2005; 151(6): 1741 - 1750. [Abstract] [Full Text] [PDF]

				M. Steiner-Mosonyi, C. Creuzenet, R. A. B. Keates, B. R. Strub, and D. Mangroo The Pseudomonas aeruginosa Initiation Factor IF-2 Is Responsible for Formylation-independent Protein Initiation in P. aeruginosa J. Biol. Chem., December 10, 2004; 279(50): 52262 - 52269. [Abstract] [Full Text] [PDF]

				M. Steiner-Mosonyi, D. M. Leslie, H. Dehghani, J. D. Aitchison, and D. Mangroo Utp8p Is an Essential Intranuclear Component of the Nuclear tRNA Export Machinery of Saccharomyces cerevisiae J. Biol. Chem., August 22, 2003; 278(34): 32236 - 32245. [Abstract] [Full Text] [PDF]

				C. MAYER, A. STORTCHEVOI, C. KOHRER, U. VARSHNEY, and U.L. RAJBHANDARY Initiator tRNA and Its Role in Initiation of Protein Synthesis Cold Spring Harb Symp Quant Biol, January 1, 2001; 66(0): 195 - 206. [Abstract] [PDF]

				D. T. Newton, C. Creuzenet, and D. Mangroo Formylation Is Not Essential for Initiation of Protein Synthesis in All Eubacteria J. Biol. Chem., August 6, 1999; 274(32): 22143 - 22146. [Abstract] [Full Text] [PDF]

				V. Ramesh, S. Gite, Y. Li, and U. L. RajBhandary Suppressor mutations in Escherichia coli methionyl-tRNA formyltransferase: Role of a 16-amino acid insertion module in initiator tRNA recognition PNAS, December 9, 1997; 94(25): 13524 - 13529. [Abstract] [Full Text] [PDF]

				X.-Q. Wu and U. L. RajBhandary Effect of the Amino Acid Attached to Escherichia coli Initiator tRNA on Its Affinity for the Initiation Factor IF2 and on the IF2 Dependence of Its Binding to the Ribosome J. Biol. Chem., January 17, 1997; 272(3): 1891 - 1895. [Abstract] [Full Text] [PDF]

				J.-M. Guillon, S. Heiss, J. Soutourina, Y. Mechulam, S. Laalami, M. Grunberg-Manago, and S. Blanquet Interplay of Methionine tRNAs with Translation Elongation Factor Tu and Translation Initiation Factor 2in Escherichia coli J. Biol. Chem., September 13, 1996; 271(37): 22321 - 22325. [Abstract] [Full Text] [PDF]

				S. Li, N. V. Kumar, U. Varshney, and U. L. RajBhandary Important Role of the Amino Acid Attached to tRNA in Formylation and in Initiation of Protein Synthesis in Escherichia coli J. Biol. Chem., January 12, 1996; 271(2): 1022 - 1028. [Abstract] [Full Text] [PDF]

				S. Thanedar, N. V. Kumar, and U. Varshney The Fate of the Initiator tRNAs Is Sensitive to the Critical Balance between Interacting Proteins J. Biol. Chem., June 30, 2000; 275(27): 20361 - 20367. [Abstract] [Full Text] [PDF]