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

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

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 Role of the Hemagglutinin-Neuraminidase Protein in the Mechanism of Paramyxovirus-Cell Membrane Fusion

2002 ◽  
Vol 76 (24) ◽  
pp. 13028-13033 ◽  
Author(s):  
Toru Takimoto ◽  
Garry L. Taylor ◽  
Helen C. Connaris ◽  
Susan J. Crennell ◽  
Allen Portner
Keyword(s):  
Plasma Membrane ◽  
Membrane Fusion ◽  
Conformational Changes ◽  
Hydrophobic Surface ◽  
Cellular Receptor ◽  
Virus Attachment ◽  
Acetylneuraminic Acid ◽  
Specific Manner ◽  
Β Sheet

ABSTRACT Paramyxovirus infects cells by initially attaching to a sialic acid-containing cellular receptor and subsequently fusing with the plasma membrane of the cells. Hemagglutinin-neuraminidase (HN) protein, which is responsible for virus attachment, interacts with the fusion protein in a virus type-specific manner to induce efficient membrane fusion. To elucidate the mechanism of HN-promoted membrane fusion, we characterized a series of Newcastle disease virus HN proteins whose surface residues were mutated. Fusion promotion activity was substantially altered in only the HN proteins with a mutation in the first or sixth β sheet. These regions overlap the large hydrophobic surface of HN; thus, the hydrophobic surface may contain the fusion promotion domain. Furthermore, a comparison of the HN structure crystallized alone or in complex with 2-deoxy-2,3-dehydro-N-acetylneuraminic acid revealed substantial conformational changes in several loops within or near the hydrophobic surface. Our results suggest that the binding of HN protein to the receptor induces the conformational change of residues near the hydrophobic surface of HN protein and that this change triggers the activation of the F protein, which initiates membrane fusion.

A role for the beta-subunit in the expression of functional Na+-K+-ATPase in Xenopus oocytes

1989 ◽  
Vol 257 (5) ◽  
pp. C851-C858 ◽  
Author(s):  
K. Geering ◽  
I. Theulaz ◽  
F. Verrey ◽  
M. T. Hauptle ◽  
B. C. Rossier
Keyword(s):  
Plasma Membrane ◽  
Conformational Changes ◽  
Structural Rearrangement ◽  
Cellular Systems ◽  
Beta Subunit ◽  
Alpha Subunit ◽  
Functional Maturation ◽  
Unique System

In all cellular systems studied so far, the catalytic alpha- and the glycosylated beta-subunit of Na+-K+-ATPase are coordinately synthesized and are assembled into stoichiometric alpha, beta-complexes. In contrast to these data, in this study we show that the fully grown oocyte of Xenopus laevis synthesizes much less beta-subunit than alpha-subunit. The alpha-subunit produced in excess over the beta-subunit is membrane associated but highly trypsin sensitive and can be compared with the immature alpha-subunit population identified in epithelial cells immediately after synthesis (K. Geering, J. P. Kraehenbuhl, and B.C. Rossier, J. Cell Biol. 105: 2613-2619, 1987). The Xenopus oocyte thus turns out to be a unique system to study the functional role of the beta-subunit. Injection of beta-subunit-specific mRNA transcribed in vitro from a beta-cDNA clone (derived from Xenopus kidney, A6 cells) into oocytes results in translation of a glycosylated beta-subunit. The synthesis of this exogenous beta-subunit increases significantly the proportion of trypsin-resistant oocyte alpha-subunits able to perform cation-dependent conformational changes. In addition, 25-65% more ouabian binding sites are expressed at the plasma membrane in beta-mRNA-injected oocytes. In contrast, newly synthesized alpha-subunit translated after injection of size-fractionated mRNA enriched in alpha-mRNA remains trypsin sensitive as the oocyte alpha-subunit. These data suggest that association of the beta-subunit to the alpha-subunit provokes a structural rearrangement of the alpha-subunit that might be a first step toward the functional maturation of the Na+-K+-ATPase and its expression at the plasma membrane.

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