Initiation of transcription at the bacterial glnAp2 promoter by purified E. coli components is facilitated by enhancers.

Abstract:

:The initiation of transcription from the nitrogen-regulated promoter glnAp2 requires RNA polymerase containing sigma 54, the transcriptional activator NRI, and the protein kinase NRII, responsible for the conversion of NRI to the active NRI-phosphate. NRI-phosphate does not increase the ability of sigma 54-containing RNA polymerase to bind to the promoter, but rather stimulates the conversion of an initial promoter:polymerase complex to the transcriptionally active open complex. The presence on the DNA template of high-affinity binding sites for NRI/NRI-phosphate, normally located 130 and 100 bp upstream of the site of transcription initiation, results in a 4- to 5-fold lowering of the concentration of NRI required for the formation of the open complex. These high-affinity NRI binding sites facilitate open complex formation when they are moved to positions 700 bp further upstream or 950 bp downstream of glnAp2 on linear DNA templates.

journal_name

Cell

journal_title

Cell

authors

Ninfa AJ,Reitzer LJ,Magasanik B

doi

10.1016/0092-8674(87)90170-x

subject

Has Abstract

pub_date

1987-09-25 00:00:00

pages

1039-46

issue

7

eissn

0092-8674

issn

1097-4172

pii

0092-8674(87)90170-X

journal_volume

50

pub_type

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