The antiterminator RNA of phage HK022

The put sites of phage HK022 increase the processivity of transcription and thereby promote the expression of viral genes that are located downstream of transcription terminators. RNA polymerase molecules that have traversed a put site are converted to a terminator-resistant form by the put transcri...

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Bibliographic Details
Published in:Journal of molecular biology 1997-10, Vol.272 (5), p.677-687
Main Authors: Banik-Maiti, Sarbani, King, Rodney A, Weisberg, Robert A
Format: Article
Language:English
Subjects:
bacteriophage HK022
Bacteriophage lambda - genetics
Base Composition
Base Sequence
DNA, Viral - chemistry
DNA-Directed RNA Polymerases - genetics
DNA-Directed RNA Polymerases - metabolism
Electrophoresis, Polyacrylamide Gel
Gene Expression Regulation, Viral - genetics
Molecular Sequence Data
Mutation - genetics
Nucleic Acid Conformation
regulatory RNA
Ribonuclease T1 - metabolism
RNA polymerase
RNA, Messenger - chemistry
RNA, Messenger - genetics
RNA, Messenger - metabolism
RNA, Viral - chemistry
RNA, Viral - genetics
RNA, Viral - metabolism
transcription termination
Transcription, Genetic - genetics
transcriptional regulatory elements
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Summary:The put sites of phage HK022 increase the processivity of transcription and thereby promote the expression of viral genes that are located downstream of transcription terminators. RNA polymerase molecules that have traversed a put site are converted to a terminator-resistant form by the put transcript. We analyzed the structure and function of put transcripts by determining the effects of put mutations on terminator readthrough, and by probing wild-type and mutant put RNAs with structure-specific nucleases. The results support the prediction that the secondary structure of the active transcript consists of two hairpin stems that are separated by a single unpaired base. The identity of bases in certain bulges and internal loops is important for activity, while that of most bases in the terminal loops is not. Many bases in the stems can be replaced with little or no effect on activity provided that base-pairing is maintained.
ISSN:0022-2836
1089-8638
DOI:10.1006/jmbi.1997.1251