Abstract
Bacteriophage T4 mRNAs are markedly stabilized, both chemically and functionally, in an Escherichia coli strain deficient in the RNA-processing endonuclease RNase E. The functional stability of total T4 messages increased 6-fold; we were unable to detect a T4 message whose functional stability was not increased. There was a 4-fold increase in the chemical stability of total T4 RNA. The degree of chemical stabilization of six specific T4 mRNAs examined varied from a maximum of 28-fold to a minimum of 1.5-fold. In the RNase E-deficient strain, several minutes delay and a slower rate of progeny production led to a reduction in final phage yield of approximately 50%. Although the effect of the rne temperature-sensitive mutation could be indirect, the simplest interpretation of our results is that RNase E acts directly in the degradation of many T4 mRNAs.
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{'key': '2021111320071422000_4.5.873.37', 'first-page': '7478', 'article-title': 'Primary structure of T4 DNA polymerase.', 'volume': '263', 'year': '1988', 'journal-title': 'J. Biol. Chem.'}
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Dates
Type | When |
---|---|
Created | 18 years, 2 months ago (June 5, 2007, 5:15 p.m.) |
Deposited | 3 years, 9 months ago (Nov. 13, 2021, 11:07 p.m.) |
Indexed | 1 year, 10 months ago (Oct. 29, 2023, 4:58 a.m.) |
Issued | 35 years, 4 months ago (May 1, 1990) |
Published | 35 years, 4 months ago (May 1, 1990) |
Published Online | 35 years, 4 months ago (May 1, 1990) |
Published Print | 35 years, 4 months ago (May 1, 1990) |
@article{Mudd_1990, title={Escherichia coli RNase E has a role in the decay of bacteriophage T4 mRNA.}, volume={4}, ISSN={1549-5477}, url={http://dx.doi.org/10.1101/gad.4.5.873}, DOI={10.1101/gad.4.5.873}, number={5}, journal={Genes & Development}, publisher={Cold Spring Harbor Laboratory}, author={Mudd, E A and Carpousis, A J and Krisch, H M}, year={1990}, month=may, pages={873–881} }