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PMID: 4568726 Published · ppublish English Journal Article

Regulation of macromolecular biosynthesis in a mutant of Escherichia coli defective in membrane phospholipid biosynthesis.

Glaser M, Bayer WH, Bell RM, Vagelos PR

Abstract

Nucleic acid and protein synthesis were studied in temperature-sensitive mutants defective in phospholipid synthesis. The defect is due to a single mutation in glycerol 3-phosphate acyltransferase (EC 2.3.1.15). The results show that at the restrictive temperature not only does phospholipid synthesis cease, but DNA, RNA, and protein synthesis also cease. Active transport continues, however, indicating that the cells do not become leaky or lose their energy supply. These results suggest that phospholipid synthesis is coupled to DNA, RNA, and protein synthesis.

MeSH Terms
Acyltransferases Bacterial Proteins/biosynthesis Carbon Isotopes DNA, Bacterial/biosynthesis Escherichia coli/growth & development,metabolism Glycerophosphates/metabolism Glycosides Kinetics Leucine/metabolism Membranes Mutation Phosphates/metabolism Phospholipids/biosynthesis Phosphorus Isotopes RNA, Bacterial/biosynthesis Temperature Thymidine/metabolism Tritium Uracil/metabolism
Chemicals
Bacterial Proteins Carbon Isotopes DNA, Bacterial Glycerophosphates Glycosides Phosphates Phospholipids Phosphorus Isotopes RNA, Bacterial Tritium Uracil Acyltransferases Leucine Thymidine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Glaser M
Bayer W H
Bell R M
Vagelos P R
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39 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1973-02-00
Pages
385-9
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC433265
Subset
IM
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