Interaction Between the Phage HK022 Nun Protein and the nut RNA of Phage λ

The nun gene product of prophage HK022 excludes phage λ infection by blocking the expression of genes downstream from the λ nut sequence. The Nun protein functions both by competing with λ N transcription-antitermination protein and by actively inducing transcription termination on the λ chromosome....

Full description

Saved in:
Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1995-12, Vol.92 (26), p.12131-12135
Main Authors: Chattopadhyay, S, Hung, S C, Stuart, A C, Palmer, 3rd, A G, Garcia-Mena, J, Das, A, Gottesman, M E
Format: Article
Language:English
Subjects:
Bacteriophage lambda - genetics
Bacteriophage lambda - metabolism
Bacteriophages
Base Sequence
Biochemistry
Coliphages - genetics
Coliphages - metabolism
Gels
Genes, Viral
Genetic mutation
Kinetics
Magnetic Resonance Spectroscopy
Molecular Sequence Data
Nucleotides
Nuns
Nuts
Oligoribonucleotides
phage HK022
phage lambda
Proteins
Protons
Ribonucleases
Ribonucleic acid
RNA
RNA, Viral - biosynthesis
RNA, Viral - chemistry
RNA, Viral - metabolism
Spectroscopy
Transcription Factors - metabolism
Transcription, Genetic
Viral Proteins - metabolism
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The nun gene product of prophage HK022 excludes phage λ infection by blocking the expression of genes downstream from the λ nut sequence. The Nun protein functions both by competing with λ N transcription-antitermination protein and by actively inducing transcription termination on the λ chromosome. We demonstrate that Nun binds directly to a stem-loop structure within nut RNA, boxB, which is also the target for the N antiterminator. The two proteins show comparable affinities for boxB and they compete with each other. Their interactions with boxB are similar, as shown by RNase protection experiments, NMR spectroscopy, and analysis of boxB mutants. Each protein binds the 5' strand of the boxB stem and the adjacent loop. The stem does not melt upon the binding of Nun or N, as the 3' strand remains sensitive to a double-strand-specific RNase. The binding of RNA partially protects Nun from proteolysis and changes its NMR spectra. Evidently, although Nun and N bind to the same surface of boxB RNA, their respective complexes interact differently with RNA polymerase, inducing transcription termination or antitermination, respectively.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.92.26.12131