Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Frances M. Antommattei"'
Autor:
Frances M, Antommattei, Robert M, Weis
Publikováno v:
The Enzymes. 24
The methyltransferase CheR catalyzes methyl group transfer from S-adenosyl-l-methionine to specific glutamic acid side chains of bacterial chemoreceptors, referred to as the methyl-accepting chemotaxis proteins (MCPs). A second enzyme, the methyleste
Autor:
Anthony L. Shrout, David J. Montefusco, Tatiana Y. Besschetnova, Frances M. Antommattei, Robert M. Weis, Abdalin E. Asinas
All cells possess transmembrane signaling systems that function in the environment of the lipid bilayer. In the Escherichia coli chemotaxis pathway, the binding of attractants to a two-dimensional array of receptors and signaling proteins simultaneou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94e5311b41696b131691920d37032f00
https://europepmc.org/articles/PMC2527904/
https://europepmc.org/articles/PMC2527904/
Publikováno v:
BMC Genomics
BMC Genomics, Vol 9, Iss 1, p 471 (2008)
BMC Genomics, Vol 9, Iss 1, p 471 (2008)
Background Geobacter species are δ-Proteobacteria and are often the predominant species in a variety of sedimentary environments where Fe(III) reduction is important. Their ability to remediate contaminated environments and produce electricity makes
Autor:
Frances M. Antommattei, Robert M. Weis
The methyltransferase CheR catalyzes methyl group transfer from S-adenosyl-l-methionine to specific glutamic acid side chains of bacterial chemoreceptors, referred to as the methyl-accepting chemotaxis proteins (MCPs). A second enzyme, the methyleste
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dde21565f9672002a99bd25fae018dd8
https://doi.org/10.1016/s1874-6047(06)80014-4
https://doi.org/10.1016/s1874-6047(06)80014-4
Publikováno v:
Journal of protein chemistry. 20(4)
Hemoglobin I (HbI) from Lucina pectinata reacts with hydrogen sulfide to form the ferric sulfide complex needed to transport H2S to the bacterial endosymbiont. To further study HbI, expression studies of this protein were performed in Escherichia col
Publikováno v:
Journal of protein chemistry. 18(8)
The tropical clam Lucina pectinata contains a unique hemoglobin (HbI) which serves to transport H2S to autotrophic bacteria. The cDNA-derived amino acid sequence was obtained from overlapping clones containing the cDNA that codes for HbI. The reverse
Publikováno v:
Journal of Bacteriology. 187:811-811
Adaptation in the chemosensory pathways of bacteria like Escherichia coli is mediated by the enzyme-catalyzed methylation (and demethylation) of glutamate residues in the signaling domains of methyl-accepting chemotaxis proteins (MCPs). MCPs can be m