Yeast plasma-membrane H+-ATPase: The role of cysteine residues

1996 ◽  
Vol 41 (1) ◽  
pp. 119-121 ◽  
Author(s):  
V. V. Petrov ◽  
J. P. Pardo ◽  
C. W. Slayman
Keyword(s):  
Plasma Membrane ◽  
Cysteine Residues ◽  
Yeast Plasma Membrane

Conformational Changes of Yeast Plasma Membrane H+-ATPase during Activation by Glucose:  Role of Threonine-912 in the Carboxy-Terminal Tail†

Biochemistry ◽  
2005 ◽  
Vol 44 (50) ◽  
pp. 16624-16632 ◽  
Author(s):  
Silvia Lecchi ◽  
Kenneth E. Allen ◽  
Juan Pablo Pardo ◽  
A. Brett Mason ◽  
Carolyn W. Slayman
Keyword(s):  
Plasma Membrane ◽  
Conformational Changes ◽  
Yeast Plasma Membrane ◽  
Carboxy Terminal

scholarly journals Functional Role of Charged Residues in the Transmembrane Segments of the Yeast Plasma Membrane H+-ATPase

2000 ◽  
Vol 275 (21) ◽  
pp. 15709-15716 ◽  
Author(s):  
Valery V. Petrov ◽  
Kristine P. Padmanabha ◽  
Robert K. Nakamoto ◽  
Kenneth E. Allen ◽  
Carolyn W. Slayman
Keyword(s):  
Plasma Membrane ◽  
Functional Role ◽  
Yeast Plasma Membrane ◽  
Transmembrane Segments ◽  
Charged Residues

The role of two small proteolipids associated to the H+-ATPase from yeast plasma membrane

1994 ◽  
pp. 199-204
Author(s):  
Catherine Navarre ◽  
Serge Leterme ◽  
Michel Ghislain ◽  
André Goffeau
Keyword(s):  
Plasma Membrane ◽  
Yeast Plasma Membrane

Yeast plasma-membrane H+-ATPase: Role of cys-409 in interaction of the enzyme with NEM and FITC

1997 ◽  
Vol 42 (3) ◽  
pp. 249-250 ◽  
Author(s):  
V. V. Petrov ◽  
J. P. Pardo ◽  
C. W. Slayman
Keyword(s):  
Plasma Membrane ◽  
Yeast Plasma Membrane

scholarly journals The role of the yeast plasma membrane SPS nutrient sensor in the metabolic response to extracellular amino acids

2008 ◽  
Vol 42 (1) ◽  
pp. 215-228 ◽  
Author(s):  
Hanna Forsberg ◽  
C. Fredrik Gilstring ◽  
Arezou Zargari ◽  
Paula Martínez ◽  
Per O. Ljungdahl
Keyword(s):  
Amino Acids ◽  
Plasma Membrane ◽  
Metabolic Response ◽  
Yeast Plasma Membrane

Evaluation of the antimicrobial activity of ebselen: Role of the yeast plasma membrane H+-ATPase

2007 ◽  
Vol 21 (5) ◽  
pp. 252-264 ◽  
Author(s):  
Grace Chan ◽  
Diane Hardej ◽  
Michelle Santoro ◽  
Cesar Lau-Cam ◽  
Blase Billack
Keyword(s):  
Antimicrobial Activity ◽  
Plasma Membrane ◽  
Yeast Plasma Membrane

scholarly journals The role of cysteine residues in glucose-transporter-GLUT1-mediated transport and transport inhibition.

1994 ◽  
Vol 299 (3) ◽  
pp. 813-817 ◽  
Author(s):  
M Wellner ◽  
I Monden ◽  
K Keller
Keyword(s):  
Plasma Membrane ◽  
Glucose Transporter ◽  
Thiol Group ◽  
Membrane Topology ◽  
Cysteine Residues ◽  
Transport Inhibition ◽  
Transport Measurements ◽  
Glucose Transporter Glut1 ◽  
Transporter Glut1

The role of cysteine residues in transport function of the glucose transporter GLUT1 was investigated by a mutagenesis-expression strategy. Each of the six cysteine residues was individually replaced by site-directed mutagenesis. Expression of the heterologous wild-type or mutant glucose transporters and transport measurements at two hexose concentrations (50 microM and 5 mM) were undertaken in Xenopus oocytes. The catalytic activity of GLUT1 was retained, despite substitution of each single cysteine residue, which indicated that no individual residue is essential for hexose transport. This finding questions the involvement of oligomerization or intramolecular stabilization by a single disulphide bond as a prerequisite for transporter activation under basal conditions. Application of the impermeant mercurial thiol-group-reactive reagent p-chloromercuribenzenesulphonate (pCMBS) to the external or internal surface of plasma membrane demonstrated that cysteine-429, within the sixth external loop, and cysteine-207, at the beginning of the large intracellular loop which connects transmembrane segments 6 and 7, are the residues which are involved in transport inhibition by impermeant thiol-group-reactive reagents from either side of the cell. These data support the predicted membrane topology of the transport protein by transport measurements. If residues other than the cysteines at positions 429 or 207 are exposed to either side of the plasma membrane by conformational changes, they do not contribute to the transport inhibition by pCMBS. Application of pCMBS to one side of the plasma membrane also inhibited transport from the opposite direction, most likely due to the hindrance of sugar-induced interconversion of transporter conformation.

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