A novel function of RNase P from Escherichia coli: processing of a suppressor tRNA precursor.

The leuX gene of Escherichia coli codes for a suppressor tRNA and forms a single gene operon containing its own promoter and Q-independent terminator. An analysis of the in vitro processing of leuX precursor revealed that the processing of the 5' end took place in a single-step reaction catalys...

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Hauptverfasser: Nomura, T, Ishihama, A
Format: Artikel
Sprache:English
Veröffentlicht: 1988
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Research Article
Online Zugang:https://ncbi.nlm.nih.gov/pmc/articles/PMC454855/
https://ncbi.nlm.nih.gov/pubmed/3061798
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spelling pubmed-4548552005-04-27 A novel function of RNase P from Escherichia coli: processing of a suppressor tRNA precursor. Nomura, T Ishihama, A EMBO J Research Article The leuX gene of Escherichia coli codes for a suppressor tRNA and forms a single gene operon containing its own promoter and Q-independent terminator. An analysis of the in vitro processing of leuX precursor revealed that the processing of the 5' end took place in a single-step reaction catalysed by RNase P while the 3' processing involved two successive reactions. The endonucleolytic cleavage activity of the 3' precursor sequence was found to copurify with RNase P. Heat inactivation of thermosensitive RNase P from two independent E. coli mutants abolished the cleavage activity of both the 5' and 3' ends. These results altogether suggest that RNase P carries the activity of 3' end cleavage as well as that of 5' processing. In the presence of Mg2+ alone, the leuX precursor was found to be self-cleaved at a site approximately 13 nt inside from the 5' end of mature tRNA. The self-cleaved precursor tRNA was no longer processed by the 3' endonuclease, suggesting that the 3' endonuclease recognizes a specific conformation of the precursor tRNA for action. 1988-11 /pmc/articles/PMC454855/ /pubmed/3061798 Text en
institution US National Library of Medicine
collection PubMed Central
language English
format Article
topic Research Article
spellingShingle Research Article
Nomura, T
Ishihama, A
A novel function of RNase P from Escherichia coli: processing of a suppressor tRNA precursor.
description The leuX gene of Escherichia coli codes for a suppressor tRNA and forms a single gene operon containing its own promoter and Q-independent terminator. An analysis of the in vitro processing of leuX precursor revealed that the processing of the 5' end took place in a single-step reaction catalysed by RNase P while the 3' processing involved two successive reactions. The endonucleolytic cleavage activity of the 3' precursor sequence was found to copurify with RNase P. Heat inactivation of thermosensitive RNase P from two independent E. coli mutants abolished the cleavage activity of both the 5' and 3' ends. These results altogether suggest that RNase P carries the activity of 3' end cleavage as well as that of 5' processing. In the presence of Mg2+ alone, the leuX precursor was found to be self-cleaved at a site approximately 13 nt inside from the 5' end of mature tRNA. The self-cleaved precursor tRNA was no longer processed by the 3' endonuclease, suggesting that the 3' endonuclease recognizes a specific conformation of the precursor tRNA for action.
author Nomura, T
Ishihama, A
author_facet Nomura, T
Ishihama, A
author_sort Nomura, T
title A novel function of RNase P from Escherichia coli: processing of a suppressor tRNA precursor.
title_short A novel function of RNase P from Escherichia coli: processing of a suppressor tRNA precursor.
title_full A novel function of RNase P from Escherichia coli: processing of a suppressor tRNA precursor.
title_fullStr A novel function of RNase P from Escherichia coli: processing of a suppressor tRNA precursor.
title_full_unstemmed A novel function of RNase P from Escherichia coli: processing of a suppressor tRNA precursor.
title_sort novel function of rnase p from escherichia coli: processing of a suppressor trna precursor.
publishDate 1988
url https://ncbi.nlm.nih.gov/pmc/articles/PMC454855/
https://ncbi.nlm.nih.gov/pubmed/3061798
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