Leader peptidase of Escherichia coli: critical role of a small domain in membrane assembly

Science ◽  
1987 ◽  
Vol 235 (4790) ◽  
pp. 783-787 ◽  
Author(s):  
R. Dalbey ◽  
W Wickner
Keyword(s):  
Escherichia Coli ◽  
Critical Role ◽  
Membrane Assembly ◽  
Small Domain ◽  
Leader Peptidase

SATP (YaaH), a succinate–acetate transporter protein in Escherichia coli

2013 ◽  
Vol 454 (3) ◽  
pp. 585-595 ◽  
Author(s):  
Joana Sá-Pessoa ◽  
Sandra Paiva ◽  
David Ribas ◽  
Inês Jesus Silva ◽  
Sandra Cristina Viegas ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Acetic Acid ◽  
Succinic Acid ◽  
Critical Role ◽  
Amino Acid Residues ◽  
E Coli ◽  
Transporter Protein ◽  
Affinity Constants ◽  
In Trans

In the present paper we describe a new carboxylic acid transporter in Escherichia coli encoded by the gene yaaH. In contrast to what had been described for other YaaH family members, the E. coli transporter is highly specific for acetic acid (a monocarboxylate) and for succinic acid (a dicarboxylate), with affinity constants at pH 6.0 of 1.24±0.13 mM for acetic acid and 1.18±0.10 mM for succinic acid. In glucose-grown cells the ΔyaaH mutant is compromised for the uptake of both labelled acetic and succinic acids. YaaH, together with ActP, described previously as an acetate transporter, affect the use of acetic acid as sole carbon and energy source. Both genes have to be deleted simultaneously to abolish acetate transport. The uptake of acetate and succinate was restored when yaaH was expressed in trans in ΔyaaH ΔactP cells. We also demonstrate the critical role of YaaH amino acid residues Leu131 and Ala164 on the enhanced ability to transport lactate. Owing to its functional role in acetate and succinate uptake we propose its assignment as SatP: the Succinate–Acetate Transporter Protein.

Critical Role of the Acceptor Stem of tRNAsMet in their Aminoacylation by Escherichia coli Methionyl-tRNA Synthetase

1993 ◽  
Vol 229 (1) ◽  
pp. 26-36 ◽  
Author(s):  
Thierry Meinnel ◽  
Yves Mechulam ◽  
Christine Lazennec ◽  
Sylvain Blanquet ◽  
Guy Fayat
Keyword(s):  
Escherichia Coli ◽  
Critical Role ◽  
Trna Synthetase ◽  
Acceptor Stem ◽  
Methionyl Trna Synthetase

scholarly journals The critical role of S ‐lactoylglutathione formation during methylglyoxal detoxification in Escherichia coli

2010 ◽  
Vol 78 (6) ◽  
pp. 1577-1590 ◽  
Author(s):  
Ertan Ozyamak ◽  
Susan S. Black ◽  
Claire A. Walker ◽  
Morag J. MacLean ◽  
Wendy Bartlett ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Critical Role

scholarly journals Role of Charged Residues in the Catalytic Sites of Escherichia coli ATP Synthase

2011 ◽  
Vol 2011 ◽  
pp. 1-12 ◽  
Author(s):  
Zulfiqar Ahmad ◽  
Florence Okafor ◽  
Thomas F. Laughlin
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Atp Synthase ◽  
Electrostatic Interactions ◽  
Critical Role ◽  
Phosphate Binding ◽  
Catalytic Sites ◽  
Charged Residues ◽  
Positively Charged

Here we describe the role of charged amino acids at the catalytic sites of Escherichia coli ATP synthase. There are four positively charged and four negatively charged residues in the vicinity of of E. coli ATP synthase catalytic sites. Positive charges are contributed by three arginine and one lysine, while negative charges are contributed by two aspartic acid and two glutamic acid residues. Replacement of arginine with a neutral amino acid has been shown to abrogate phosphate binding, while restoration of phosphate binding has been accomplished by insertion of arginine at the same or a nearby location. The number and position of positive charges plays a critical role in the proper and efficient binding of phosphate. However, a cluster of many positive charges inhibits phosphate binding. Moreover, the presence of negatively charged residues seems a requisite for the proper orientation and functioning of positively charged residues in the catalytic sites. This implies that electrostatic interactions between amino acids are an important constituent of initial phosphate binding in the catalytic sites. Significant loss of function in growth and ATPase activity assays in mutants generated through charge modulations has demonstrated that precise location and stereochemical interactions are of paramount importance.

scholarly journals A Critical Role of Formyl Peptide Receptors in Host Defense against Escherichia coli

2020 ◽  
Vol 204 (9) ◽  
pp. 2464-2473 ◽  
Author(s):  
Meihua Zhang ◽  
Ji-Liang Gao ◽  
Keqiang Chen ◽  
Teizo Yoshimura ◽  
Weiwei Liang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Host Defense ◽  
Critical Role ◽  
Peptide Receptors ◽  
Formyl Peptide Receptors ◽  
Formyl Peptide
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