Abstract:
:Although the ribosome is a very general catalyst, it cannot synthesize all protein sequences equally well. For example, ribosomes stall on the secretion monitor (SecM) leader peptide to regulate expression of a downstream gene. Using a genetic selection in Escherichia coli, we identified additional nascent peptide motifs that stall ribosomes. Kinetic studies show that some nascent peptides dramatically inhibit rates of peptide release by release factors. We find that residues upstream of the minimal stalling motif can either enhance or suppress this effect. In other stalling motifs, peptidyl transfer to certain aminoacyl-tRNAs is inhibited. In particular, three consecutive Pro codons pose a challenge for elongating ribosomes. The translation factor elongation factor P, which alleviates pausing at polyproline sequences, has little or no effect on other stalling peptides. The motifs that we identified are underrepresented in bacterial proteomes and show evidence of stalling on endogenous E. coli proteins.
journal_name
Proc Natl Acad Sci U S Aauthors
Woolstenhulme CJ,Parajuli S,Healey DW,Valverde DP,Petersen EN,Starosta AL,Guydosh NR,Johnson WE,Wilson DN,Buskirk ARdoi
10.1073/pnas.1219536110subject
Has Abstractpub_date
2013-03-05 00:00:00pages
E878-87issue
10eissn
0027-8424issn
1091-6490pii
1219536110journal_volume
110pub_type
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