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- W2152011513 endingPage "1284" @default.
- W2152011513 startingPage "1275" @default.
- W2152011513 abstract "The aspartate chemoreceptor Tar of Escherichia coli serves as a warm sensor that produces attractant and repellent signals upon increases and decreases in temperature, respectively. However, increased levels of methylation of the cytoplasmic domain of Tar resulting from aspartate binding convert Tar to a cold sensor with the opposite signaling behavior. Detailed analyses of the methylation sites, which are located in two separate alpha-helices (MH1 and MH2), have suggested that intra- and/or intersubunit interactions of MH1 and MH2 play a critical role in thermosensing. These interactions may be influenced by binding of aspartate, which could trigger some displacement of MH1 through the second transmembrane region (TM2). As an initial step toward understanding the role of TM2 in thermosensing, we have examined the thermosensing properties of 43 mutant Tar receptors with randomized TM2 sequences (residues 190-210). Among them, we identified one mutant receptor (Tar-I2) that functioned as a cold sensor in the absence of aspartate. This is the first example of attractant-independent inversion of thermosensing in Tar. Further analyses identified the minimal essential divergence from the wild-type Tar sequence (Q191V-W192R-Q193C) required for the inverted response. Thus, displacements of TM2 seem to influence the thermosensing function of Tar." @default.
- W2152011513 created "2016-06-24" @default.
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- W2152011513 creator A5036868997 @default.
- W2152011513 creator A5062510801 @default.
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- W2152011513 date "1999-03-01" @default.
- W2152011513 modified "2023-09-23" @default.
- W2152011513 title "Inversion of thermosensing property of the bacterial receptor tar by mutations in the second transmembrane region" @default.
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- W2152011513 doi "https://doi.org/10.1006/jmbi.1999.2555" @default.
- W2152011513 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10064695" @default.
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