Cleavage of the sarcin-ricin loop of 23S rRNA differentially affects EF-G and EF-Tu binding.

Abstract:

:Ribotoxins are potent inhibitors of protein biosynthesis and inactivate ribosomes from a variety of organisms. The ribotoxin alpha-sarcin cleaves the large 23S ribosomal RNA (rRNA) at the universally conserved sarcin-ricin loop (SRL) leading to complete inactivation of the ribosome and cellular death. The SRL interacts with translation factors that hydrolyze GTP, and it is important for their binding to the ribosome, but its precise role is not yet understood. We studied the effect of alpha-sarcin on defined steps of translation by the bacterial ribosome. alpha-Sarcin-treated ribosomes showed no defects in mRNA and tRNA binding, peptide-bond formation and sparsomycin-dependent translocation. Cleavage of SRL slightly affected binding of elongation factor Tu ternary complex (EF-Tu*GTP*tRNA) to the ribosome. In contrast, the activity of elongation factor G (EF-G) was strongly impaired in alpha-sarcin-treated ribosomes. Importantly, cleavage of SRL inhibited EF-G binding, and consequently GTP hydrolysis and mRNA-tRNA translocation. These results suggest that the SRL is more critical in EF-G than ternary complex binding to the ribosome implicating different requirements in this region of the ribosome during protein elongation.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

García-Ortega L,Alvarez-García E,Gavilanes JG,Martínez-del-Pozo A,Joseph S

doi

10.1093/nar/gkq151

subject

Has Abstract

pub_date

2010-07-01 00:00:00

pages

4108-19

issue

12

eissn

0305-1048

issn

1362-4962

pii

gkq151

journal_volume

38

pub_type

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