Unusual mRNA pseudoknot structure is recognized by a protein translational repressor.

Abstract:

:Translation of ribosomal proteins in the alpha operon of E. coli is repressed by one of the encoded proteins, S4; it specifically recognizes an RNA fragment containing the translational initiation site for the first gene in the operon. RNA structure mapping experiments have suggested a pseudoknot structure for the S4 binding site: the loop of a hairpin is base paired to sequences downstream of the hairpin. Here, we systematically test this proposed structure by measuring S4 binding to an extensive set of site-directed mutations that create compensatory base pair changes in potential helices. The pseudoknot folding is confirmed, and two additional, unexpected interactions within the pseudoknot are also detected. The overall structure is an unusual "double pseudoknot" linking a hairpin upstream of the ribosome binding site with sequences 2-10 codons downstream of the initiation codon. Stabilization of this structure by S4 could account for translational repression.

journal_name

Cell

journal_title

Cell

authors

Tang CK,Draper DE

doi

10.1016/0092-8674(89)90123-2

subject

Has Abstract

pub_date

1989-05-19 00:00:00

pages

531-6

issue

4

eissn

0092-8674

issn

1097-4172

pii

0092-8674(89)90123-2

journal_volume

57

pub_type

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