Tvp38, Tvp23, Tvp18 and Tvp15: Novel membrane proteins in the Tlg2-containing Golgi/endosome compartments of Saccharomyces cerevisiae

ABSTRACT Prohibitins comprise a protein family in eukaryotic cells with potential roles in senescence and tumor suppression. Phb1p and Phb2p, members of the prohibitin family in Saccharomyces cerevisiae, have been implicated in the regulation of the replicative life span of the cells and in the maintenance of mitochondrial morphology. The functional activities of these proteins, however, have not been elucidated. We demonstrate here that prohibitins regulate the turnover of membrane proteins by the m-AAA protease, a conserved ATP-dependent protease in the inner membrane of mitochondria. The m-AAA protease is composed of the homologous subunits Yta10p (Afg3p) and Yta12p (Rca1p). Deletion ofPHB1 or PHB2 impairs growth of Δyta10 or Δyta12 cells but does not affect cell growth in the presence of the m-AAA protease. A prohibitin complex with a native molecular mass of approximately 2 MDa containing Phb1p and Phb2p forms a supercomplex with them-AAA protease. Proteolysis of nonassembled inner membrane proteins by the m-AAA protease is accelerated in mitochondria lacking Phb1p or Phb2p, indicating a negative regulatory effect of prohibitins on m-AAA protease activity. These results functionally link members of two conserved protein families in eukaryotes to the degradation of membrane proteins in mitochondria.

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Expression and Purification of Membrane Proteins in Saccharomyces cerevisiae

Methods in Molecular Biology - Expression, Purification, and Structural Biology of Membrane Proteins ◽

10.1007/978-1-0716-0373-4_4 ◽

2020 ◽

pp. 47-61

Author(s):

Martin S. King ◽

Edmund R. S. Kunji

Keyword(s):

Saccharomyces Cerevisiae ◽

Membrane Proteins ◽

Expression And Purification

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Fmp30, Mdm31, and Mdm32 Function in Ups1-Independent Cardiolipin Accumulation Under Low Phosphatidylethanolamine Conditions

Contact ◽

10.1177/2515256418764043 ◽

2018 ◽

Vol 1 ◽

pp. 251525641876404

Author(s):

Non Miyata ◽

Osamu Kuge

Keyword(s):

Saccharomyces Cerevisiae ◽

Membrane Proteins ◽

Phosphatidic Acid ◽

Yeast Saccharomyces Cerevisiae ◽

Inner Membrane ◽

Mitochondrial Inner Membrane ◽

Per Se

Maintenance of the cardiolipin (CL) level largely depends on Ups1-Mdm35 complex-mediated intramitochondrial phosphatidic acid transfer. In addition, the presence of an alternative CL accumulation pathway has been suggested in the yeast Saccharomyces cerevisiae. This pathway is independent of the Ups1-Mdm35 complex and stimulated by loss of Ups2, which forms a complex with Mdm35 and mediates intramitochondrial transfer of phosphatidylserine for phosphatidylethanolamine synthesis. Recently, we found that the alternative CL accumulation pathway is enhanced by a lowered phosphatidylethanolamine level, not by loss of Ups2 per se, and depends on three mitochondrial inner membrane proteins, Fmp30, Mdm31, and Mdm32.

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Plasma membrane proteins Yro2 and Mrh1 are required for acetic acid tolerance in Saccharomyces cerevisiae

Applied Microbiology and Biotechnology ◽

10.1007/s00253-014-6278-2 ◽

2014 ◽

Vol 99 (6) ◽

pp. 2805-2814 ◽

Cited By ~ 12

Author(s):

Akiko Takabatake ◽

Nozomi Kawazoe ◽

Shingo Izawa

Keyword(s):

Saccharomyces Cerevisiae ◽

Acetic Acid ◽

Plasma Membrane ◽

Membrane Proteins ◽

Acid Tolerance ◽

Acetic Acid Tolerance ◽

Plasma Membrane Proteins

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Retrieval of Resident Late-Golgi Membrane Proteins from the Prevacuolar Compartment of Saccharomyces cerevisiae Is Dependent on the Function of Grd19p

The Journal of Cell Biology ◽

10.1083/jcb.140.3.577 ◽

1998 ◽

Vol 140 (3) ◽

pp. 577-590 ◽

Cited By ~ 67

Author(s):

Wolfgang Voos ◽

Tom H. Stevens

Keyword(s):

Saccharomyces Cerevisiae ◽

Membrane Proteins ◽

Membrane Protein ◽

Protein Localization ◽

Transport Processes ◽

Carboxypeptidase Y ◽

Golgi Membrane ◽

Cytosolic Domain ◽

Prevacuolar Compartment ◽

Vacuolar Protein

The dynamic vesicle transport processes at the late-Golgi compartment of Saccharomyces cerevisiae (TGN) require dedicated mechanisms for correct localization of resident membrane proteins. In this study, we report the identification of a new gene, GRD19, involved in the localization of the model late-Golgi membrane protein A-ALP (consisting of the cytosolic domain of dipeptidyl aminopeptidase A [DPAP A] fused to the transmembrane and lumenal domains of the alkaline phosphatase [ALP]), which localizes to the yeast TGN. A grd19 null mutation causes rapid mislocalization of the late-Golgi membrane proteins A-ALP and Kex2p to the vacuole. In contrast to previously identified genes involved in late-Golgi membrane protein localization, grd19 mutations cause only minor effects on vacuolar protein sorting. The recycling of the carboxypeptidase Y sorting receptor, Vps10p, between the TGN and the prevacuolar compartment is largely unaffected in grd19Δ cells. Kinetic assays of A-ALP trafficking indicate that GRD19 is involved in the process of retrieval of A-ALP from the prevacuolar compartment. GRD19 encodes a small hydrophilic protein with a predominantly cytosolic distribution. In a yeast mutant that accumulates an exaggerated form of the prevacuolar compartment (vps27), Grd19p was observed to localize to this compartment. Using an in vitro binding assay, Grd19p was found to interact physically with the cytosolic domain of DPAP A. We conclude that Grd19p is a component of the retrieval machinery that functions by direct interaction with the cytosolic tails of certain TGN membrane proteins during the sorting/budding process at the prevacuolar compartment.

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Channel-forming activities of peroxisomal membrane proteins from the yeast Saccharomyces cerevisiae

FEBS Journal ◽

10.1111/j.1742-4658.2009.06903.x ◽

2009 ◽

Vol 276 (6) ◽

pp. 1698-1708 ◽

Cited By ~ 19

Author(s):

Silke Grunau ◽

Sabrina Mindthoff ◽

Hanspeter Rottensteiner ◽

Raija T. Sormunen ◽

J. Kalervo Hiltunen ◽

...

Keyword(s):

Saccharomyces Cerevisiae ◽

Membrane Proteins ◽

Peroxisomal Membrane ◽

Yeast Saccharomyces Cerevisiae

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Immunoisolaton of the Yeast Golgi Subcompartments and Characterization of a Novel Membrane Protein, Svp26, Discovered in the Sed5-Containing Compartments

Molecular and Cellular Biology ◽

10.1128/mcb.25.17.7696-7710.2005 ◽

2005 ◽

Vol 25 (17) ◽

pp. 7696-7710 ◽

Cited By ~ 40

Author(s):

Hironori Inadome ◽

Yoichi Noda ◽

Hiroyuki Adachi ◽

Koji Yoda

Keyword(s):

Saccharomyces Cerevisiae ◽

Endoplasmic Reticulum ◽

Membrane Proteins ◽

Golgi Apparatus ◽

Membrane Protein ◽

Considerable Portion ◽

Marker Proteins ◽

Evolutionarily Conserved ◽

Golgi Compartment

ABSTRACT The Golgi apparatus consists of a set of vesicular compartments which are distinguished by their marker proteins. These compartments are physically separated in the Saccharomyces cerevisiae cell. To characterize them extensively, we immunoisolated vesicles carrying either of the SNAREs Sed5 or Tlg2, the markers of the early and late Golgi compartments, respectively, and analyzed the membrane proteins. The composition of proteins was mostly consistent with the position of each compartment in the traffic. We found six uncharacterized but evolutionarily conserved proteins and named them Svp26 (Sed5 compartment vesicle protein of 26 kDa), Tvp38, Tvp23, Tvp18, Tvp15 (Tlg2 compartment vesicle proteins of 38, 23, 18, and 15 kDa), and Gvp36 (Golgi vesicle protein of 36 kDa). The localization of Svp26 in the early Golgi compartment was confirmed by microscopic and biochemical means. Immunoprecipitation indicated that Svp26 binds to itself and a Golgi mannosyltransferase, Ktr3. In the absence of Svp26, a considerable portion of Ktr3 was mislocalized in the endoplasmic reticulum. Our data suggest that Svp26 has a novel role in retention of a subset of membrane proteins in the early Golgi compartments.

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