PMID:2182127
| Citation |
Sumpter, VG, Tate, WP and Nierhaus, KH (1990) The complex between ribosomal proteins and aminoacyl-tRNA: the interactions and hydrolytic activities are not confined to the proteins L2 and L16 of Escherichia coli ribosomes. Biochim. Biophys. Acta 1048:265-9 |
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| Abstract |
The capacity of some Escherichia coli (E. coli) ribosomal proteins to bind to tRNA and to hydrolyse their aminoacylated derivatives has been analysed. The following results were obtained: (1) The basic proteins L2, L16 and L33 and S20 bound f[3H]Met-tRNA to a similar extent as the total proteins from 30 S (TP30) or 50 S (TP50) when tested by nitrocellulose filtration, in contrast to the more acidic proteins L7/L12 and S8. (2) The proteins of the peptidyltransferase centre, L2 and L16, showed no distinct specificity, binding various charged tRNAs from E. coli and Saccharomyces cerevisiae (S. cerevisiae). (3) A number of isolated ribosomal proteins hydrolysed aminoacyl-tRNA as assessed by trichloroacetic acid precipitation, in contrast to the TP30 and TP50. (4) The loss of radiolabel from Ac[14C]Phe-tRNA and from [14C]tRNA in the presence of these proteins could not be prevented by RNasin, a ribonuclease inhibitor, whereas that mediated by a sample of non-RNase-free bovine serum albumin was inhibited. (5) When double-labelled, Ac[3H]Phe-[14C]tRNA was incubated with L2 both radiolabels were lost, indicating that this potential candidate for a peptidyltransferase enzyme does not specifically cleave the ester bond between the aminoacyl residue and the tRNA. |
| Links | |
| Keywords |
Escherichia coli/metabolism; Hydrolysis; Protein Binding; RNA, Transfer, Amino Acyl/metabolism; Ribosomal Proteins/isolation & purification; Ribosomal Proteins/metabolism; Ribosomes/metabolism; Saccharomyces cerevisiae/metabolism |
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