Abstract：
:E. coli sigma 54 protein confers on promoters containing its recognition sequence the ability to be activated from distant DNA sites. Its functional domains include two leucine zipper motifs, an acidic region, and a glutamine-rich domain. Several domains were disrupted and the assembly of mutant transcription complexes was probed in vivo by footprinting. Promoter recognition was seen to depend on a C-terminal region containing a prokaryotic helix-turn-helix motif. Within the resulting stable closed complex, two leucine zipper motifs assist in positioning the sigma 54 polymerase near the DNA region that must be melted upon activation. Finally, DNA opening depends on the sigma 54 acid domain. The uncoupling of promoter recognition from DNA melting, mediated by the unusual domain structure of this prokaryotic protein, may be responsible for sigma 54,s ability to mediate activation from distant sites.
journal_name
Celljournal_title
Cellauthors
Sasse-Dwight S,Gralla JDdoi
10.1016/0092-8674(90)90269-ksubject
Has Abstractpub_date
1990-09-07 00:00:00pages
945-54issue
5eissn
0092-8674issn
1097-4172pii
0092-8674(90)90269-Kjournal_volume
62pub_type
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