The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Sensory transduction in Escherichia coli: two complementary pathways of information processing that involve methylated proteins.
Open accessAbstract
The properties of two classes of behavioral mutants of Escherichia coli (called tsr and tar) are described. The mutations in these strains define two complementary pathways of information flow in bacterial chemotaxis: behavioral responses to one set of stimuli are defective in tsr mutants, while responses to a complementary set of stimuli are defective in tar mutants. A double mutant containing both genetic lesions is defective in responses to all stimuli tested. The behavioral defects are shown to correlate with alterations in the properties of a methylation reaction involved in chemotaxis. Two independent sets of methyl-accepting proteins are demonstrated in the wild type, each set functioning in one of the two pathways mentioned above. Methylation of one set of proteins is defective in tsr mutants, while methylation of the complementary set is defective in tar mutants. The double mutant shows no methylation of either set. The relationship between the genetic loci (tsr and tar) and the methyl-accepting proteins is discussed.
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Cites
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
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Quantitative Film Detection of 3H and 14C in Polyacrylamide Gels by Fluorography
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The Gradient-Sensing Mechanism in Bacterial Chemotaxis
Macnab, R. M., & Koshland, D. E. (1972) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.69.9.2509 · Cited by 917
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Self-citationMethylation of a membrane protein involved in bacterial chemotaxis.
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Cited by
Linkage map of Escherichia coli K-12, edition 6
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Metadata
- Authors
- Springer, M. S., Goy, M. F., & Adler, J.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1977-08
- Volume
- 74
- Issue
- 8
- Pages
- 3312-3316
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2021645499
- Cited by
- 280
- References
- 10
- FWCI
- 15.48
- Type
- journal article
- Language
- en
- Open access
- green
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