RNA polymerase efficiently transcribes through DNA-scaffolded, cooperative bacteriophage repressor complexes.
atomic force microscopy
bacteriophage repressors
roadblock efficiency
topology
transcription
Journal
FEBS letters
ISSN: 1873-3468
Titre abrégé: FEBS Lett
Pays: England
ID NLM: 0155157
Informations de publication
Date de publication:
08 2022
08 2022
Historique:
revised:
17
06
2022
received:
22
03
2022
accepted:
19
06
2022
pubmed:
13
7
2022
medline:
31
8
2022
entrez:
12
7
2022
Statut:
ppublish
Résumé
DNA can act as a scaffold for the cooperative binding of protein oligomers. For example, the phage 186 CI repressor forms a wheel of seven dimers wrapped in DNA with specific binding sites, while phage λ CI repressor dimers bind to two well-separated sets of operators, forming a DNA loop. Atomic force microscopy was used to measure transcription elongation by Escherichia coli RNA polymerase (RNAP) through these protein complexes. 186 CI, or λ CI, bound along unlooped DNA negligibly interfered with transcription by RNAP. Wrapped and looped topologies induced by these scaffolded, cooperatively bound repressor oligomers did not form significantly better roadblocks to transcription. Thus, despite binding with high affinity, these repressors are not effective roadblocks to transcription.
Identifiants
pubmed: 35819073
doi: 10.1002/1873-3468.14447
pmc: PMC9491066
mid: NIHMS1833100
doi:
Substances chimiques
Viral Regulatory and Accessory Proteins
0
DNA
9007-49-2
DNA-Directed RNA Polymerases
EC 2.7.7.6
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
1994-2006Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM084070
Pays : United States
Informations de copyright
© 2022 Federation of European Biochemical Societies.
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