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PMID: 3671066 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Purification in an active form of the phage phi 29 protein p4 that controls the viral late transcription.

Nucleic acids research ·Vol. 15 ·No. 19 ·1987-10-12 ·Pages 7781-93

Barthelemy I, Lázaro JM, Méndez E, Mellado RP, Salas M

Abstract

The phage phi 29 protein p4, that controls viral late transcription, was highly purified from Escherichia coli cells harbouring a gene 4-containing plasmid. This protein, representing about 6% of the total cellular protein, was obtained in a highly purified form. The protein was characterized as p4 by amino acid analysis and NH2-terminal sequence determination. The purified protein was active in an in vitro transcription assay, allowing specific initiation of transcription at the phi 29 A3 late promoter in the presence of Bacillus subtilis sigma 43-RNA polymerase holoenzyme.

MeSH Terms
Amino Acids/analysis Bacteriophages/analysis,physiology DNA-Directed RNA Polymerases/metabolism Promoter Regions, Genetic Recombinant Proteins/physiology Transcription Factors/isolation & purification,physiology Transcription, Genetic Viral Proteins
Chemicals
Amino Acids Recombinant Proteins Transcription Factors Viral Proteins p4 protein, Bacteriophage phi 29 DNA-Directed RNA Polymerases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Barthelemy I
Centro de Biología Molecular (CSIC-UAM), Universidad Autónoma, Madrid, Spain.
Lázaro J M
Méndez E
Mellado R P
Salas M
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
DOI
10.1093/nar/15.19.7781
Published
1987-10-12
Pages
7781-93
Language
English
Region
England
NLM ID
0411011
PMCID
PMC306307
Subset
IM
Grants
NIGMS NIH HHS · 2 R01 GM27242-08 · United States
External Links
PubMed source DOI: 10.1093/nar/15.19.7781 PMC Full Text View journal details
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