Thermosensing properties of mutant aspartate chemoreceptors with methyl-accepting sites replaced singly or multiply by alanine.

The aspartate chemoreceptor Tar has a thermosensing function that is modulated by covalent modification of its four methylation sites (Gln295, Glu302, Gln309, and Glu491). Without posttranslational deamidation, Tar has no thermosensing ability. When Gln295 and Gln309 are deamidated to Glu, the unmet...

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Vydáno v:	J Bacteriol
Hlavní autoři:	Nishiyama, S, Nara, T, Homma, M, Imae, Y, Kawagishi, I
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	American Society for Microbiology (ASM) 1997
Témata:	Research Article
On-line přístup:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC179581/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/9352902/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.179.21.6573-6580.1997
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