Unknown

Dataset Information

0

The bacteriophage T4 late-transcription coactivator gp33 binds the flap domain of Escherichia coli RNA polymerase.


ABSTRACT: Transcription of bacteriophage T4 late genes requires concomitant DNA replication. T4 late promoters, which consist of a single 8-bp -10 motif, are recognized by a holoenzyme containing Escherichia coli RNA polymerase core and the T4-encoded promoter specificity subunit, gp55. Initiation of transcription at these promoters by gp55-holoenzyme is inefficient, but is greatly activated by the DNA-loaded DNA polymerase sliding clamp, gp45, and the coactivator, gp33. We report that gp33 attaches to the flap domain of the Escherichia coli RNA polymerase beta-subunit and that this interaction is essential for activation. The beta-flap also mediates recognition of -35 promoter motifs by binding to sigma(70) domain 4. The results suggest that gp33 is an analogue of sigma(70) domain 4 and that gp55 and gp33 together constitute two parts of the T4 late sigma. We propose a model for the role of the gp45 sliding clamp in activation of T4 late-gene transcription.

SUBMITTER: Nechaev S 

PROVIDER: S-EPMC535105 | biostudies-literature | 2004 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

The bacteriophage T4 late-transcription coactivator gp33 binds the flap domain of Escherichia coli RNA polymerase.

Nechaev Sergei S   Kamali-Moghaddam Masood M   André Estelle E   Léonetti Jean-Paul JP   Geiduschek E Peter EP  

Proceedings of the National Academy of Sciences of the United States of America 20041201 50


Transcription of bacteriophage T4 late genes requires concomitant DNA replication. T4 late promoters, which consist of a single 8-bp -10 motif, are recognized by a holoenzyme containing Escherichia coli RNA polymerase core and the T4-encoded promoter specificity subunit, gp55. Initiation of transcription at these promoters by gp55-holoenzyme is inefficient, but is greatly activated by the DNA-loaded DNA polymerase sliding clamp, gp45, and the coactivator, gp33. We report that gp33 attaches to th  ...[more]

Similar Datasets

| S-EPMC3250119 | biostudies-literature
| S-EPMC2672554 | biostudies-literature
| S-EPMC2953677 | biostudies-literature
| S-EPMC3503030 | biostudies-literature
| S-EPMC2536758 | biostudies-literature
| S-EPMC4027172 | biostudies-literature
| S-EPMC7472727 | biostudies-literature
| S-EPMC3234753 | biostudies-literature
| S-EPMC5221442 | biostudies-literature
| S-EPMC2930546 | biostudies-literature