Abstract：
:The 10Sa RNA, encoded by the E. coli ssrA gene, appears to modulate action of some DNA-binding proteins. When ssrA is inactivated, lacZ expression from the lac operon, as well as galK from a gal operon fused to a phage lambda promoter, is reduced from that observed in bacteria wild-type for ssrA. These differences are not observed if the relevant repressor is inactive, suggesting that in the absence of 10Sa RNA binding of LacI and lambda cI repressors is enhanced. Gel mobility shifts show that 10Sa RNA binds these repressors and that an excess of 10Sa RNA competes for binding of lambda cI with a DNA fragment containing the OR2 repressor-binding sequence. Similar observations were made in studies of the E. coli LexA repressor and phage P22 C1 transcription activator proteins. These results suggest that direct interaction with 10Sa RNA may explain this modulation of protein-DNA interactions.
journal_name
Celljournal_title
Cellauthors
Retallack DM,Friedman DIdoi
10.1016/0092-8674(95)90164-7subject
Has Abstractpub_date
1995-10-20 00:00:00pages
227-35issue
2eissn
0092-8674issn
1097-4172pii
0092-8674(95)90164-7journal_volume
83pub_type
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