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

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted 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 Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Smith, K. E. Articles by Henshaw, E. C. Search for Related Content PubMed PubMed Citation Articles by Smith, K. E. Articles by Henshaw, E. C. Social Bookmarking                      What's this?

JBC, Vol. 250, Issue 17, 6880-6884, Sep, 1975

Binding of Met-tRNAf to native 40 S ribosomal subunits in Ehrlich ascites tumor cells

K. E. Smith and E. C. Henshaw

Two forms of native 40 S ribosomal subunits, distinguishable by their buoyant densities, are recovered from Ehrlich ascites cells. In this communication, we describe experiments designed to test whether Met-tRNAf is associated with either form. Our results indicate that (a) in the cell, Met-tRNAf is bound to the native 40 S subunit, and in particular, to the subunit of density 1.40 g x cm-3; (b) under the growth conditions used, less than 10% of the low density native subunits have bound Met-tRNAf; (c) the majority of the Met-tRNAf containing native 40 S subunits, isolated from sucrose gradient analyses of cell extracts, join with 60 S subunits in vitro to form 80 S monosomes only if additional ribosomal wash factors are provided; and (d) the 80 S monosomes so formed are completed initiation complexes that can form peptide bonds. These results support the hypothesis that various forms of the native 40 S subunit represent different stages in the formation of a complete initiation complex.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				R. Majumdar, A. Bandyopadhyay, and U. Maitra Mammalian Translation Initiation Factor eIF1 Functions with eIF1A and eIF3 in the Formation of a Stable 40 S Preinitiation Complex J. Biol. Chem., February 14, 2003; 278(8): 6580 - 6587. [Abstract] [Full Text] [PDF]

				A. Bandyopadhyay, T. Matsumoto, and U. Maitra Fission Yeast Int6 Is Not Essential for Global Translation Initiation, but Deletion of int6+ Causes Hypersensitivity to Caffeine and Affects Spore Formation Mol. Biol. Cell, November 1, 2000; 11(11): 4005 - 4018. [Abstract] [Full Text]

				J. Chaudhuri, D. Chowdhury, and U. Maitra Distinct Functions of Eukaryotic Translation Initiation Factors eIF1A and eIF3 in the Formation of the 40 S Ribosomal Preinitiation Complex J. Biol. Chem., June 18, 1999; 274(25): 17975 - 17980. [Abstract] [Full Text] [PDF]

				J. Chaudhuri, K. Si, and U. Maitra Function of Eukaryotic Translation Initiation Factor 1A (eIF1A) (Formerly Called eIF-4C) in Initiation of Protein Synthesis J. Biol. Chem., March 21, 1997; 272(12): 7883 - 7891. [Abstract] [Full Text] [PDF]