Multiple Forms of Methyl-accepting Chemotaxis Proteins Distinguished by a Factor in Addition to Multiple Methylation

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1981 Jan 1

PMID 7007319

Citations 23

Authors

G L Hazelbauer

P Engstrom

Affiliations

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Abstract

Methyl-accepting chemotaxis proteins are central to both the excitation and adaptation phases of chemotactic behavior. Using null mutations in the genes coding for the two major methyl-accepting proteins (tsr and tar), we identified the gene products among the membrane proteins of Escherichia coli visualized on one- and two-dimensional gels. On two-dimensional gels, both the tsr and the tar proteins appeared as a group of multiple spots arranged in two to four diagonal arrays. The multiplicity of forms could not be completely explained by the previously documented heterogeneity of the methylated proteins resulting from different numbers of methylated glutamyl residues per polypeptide chain. We suggest that there is at least one other way besides extent of methylation in which the polypeptides of a methylated protein can differ.

Citing Articles

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Functional organization of a multimodular bacterial chemosensory apparatus.

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Cellular stoichiometry of the components of the chemotaxis signaling complex.

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