Publication Date:
1999-12-22
Description:
The amino-terminal arginine-rich motif of coliphage HK022 Nun binds phage lambda nascent transcript, whereas the carboxyl-terminal domain interacts with RNA polymerase (RNAP) and blocks transcription elongation. RNA binding is inhibited by zinc (Zn2+) and stimulated by Escherichia coli NusA. To study these interactions, the Nun carboxyl terminus was extended by a cysteine residue conjugated to a photochemical cross-linker. The carboxyl terminus contacted NusA and made Zn2+-dependent intramolecular contacts. When Nun was added to a paused transcription elongation complex, it cross-linked to the DNA template. Nun may arrest transcription by anchoring RNAP to DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Watnick, R S -- Gottesman, M E -- New York, N.Y. -- Science. 1999 Dec 17;286(5448):2337-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics and Institute of Cancer Research, Columbia University, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10600743" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Azides
;
Bacterial Proteins/metabolism
;
Bacteriophage lambda/genetics/physiology
;
Cross-Linking Reagents
;
DNA, Viral/*metabolism
;
DNA-Directed RNA Polymerases/metabolism
;
Dithiothreitol/pharmacology
;
Escherichia coli/enzymology/virology
;
Escherichia coli Proteins
;
Molecular Sequence Data
;
*Peptide Elongation Factors
;
Phenanthrolines/metabolism
;
Protein Binding
;
Pyridines
;
RNA, Messenger/*metabolism
;
RNA, Viral/metabolism
;
Templates, Genetic
;
Transcription Factors/chemistry/*metabolism
;
*Transcription, Genetic
;
Transcriptional Elongation Factors
;
Viral Plaque Assay
;
Viral Proteins/chemistry/*metabolism
;
Zinc/pharmacology
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
