BibTex format

author = {Yang, Y and Darbari, VC and Zhang, N and Lu, D and Glyde, R and Wang, Y-P and Winkelman, JT and Gourse, RL and Murakami, KS and Buck, M and Zhang, X},
doi = {10.1126/science.aab1478},
journal = {Science},
pages = {882--885},
title = {Structures of the RNA polymerase-sigma(54) reveal new and conserved regulatory strategies},
url = {},
volume = {349},
year = {2015}

RIS format (EndNote, RefMan)

AB - Transcription by RNA polymerase (RNAP) in bacteria requires specific promoter recognition by σ factors. The major variant σ factor (σ54) initially forms a transcriptionally silent complex requiring specialized adenosine triphosphate–dependent activators for initiation. Our crystal structure of the 450-kilodalton RNAP-σ54 holoenzyme at 3.8 angstroms reveals molecular details of σ54 and its interactions with RNAP. The structure explains how σ54 targets different regions in RNAP to exert its inhibitory function. Although σ54 and the major σ factor, σ70, have similar functional domains and contact similar regions of RNAP, unanticipated differences are observed in their domain arrangement and interactions with RNAP, explaining their distinct properties. Furthermore, we observe evolutionarily conserved regulatory hotspots in RNAPs that can be targeted by a diverse range of mechanisms to fine tune transcription.
AU - Yang,Y
AU - Darbari,VC
AU - Zhang,N
AU - Lu,D
AU - Glyde,R
AU - Wang,Y-P
AU - Winkelman,JT
AU - Gourse,RL
AU - Murakami,KS
AU - Buck,M
AU - Zhang,X
DO - 10.1126/science.aab1478
EP - 885
PY - 2015///
SN - 0036-8075
SP - 882
TI - Structures of the RNA polymerase-sigma(54) reveal new and conserved regulatory strategies
T2 - Science
UR -
UR -
UR -
VL - 349
ER -