G
Gertrud Mannhaupt
Researcher at Ludwig Maximilian University of Munich
Publications - 18
Citations - 1279
Gertrud Mannhaupt is an academic researcher from Ludwig Maximilian University of Munich. The author has contributed to research in topics: Gene & Saccharomyces cerevisiae. The author has an hindex of 13, co-authored 18 publications receiving 1234 citations.
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Journal ArticleDOI
Rpn4p acts as a transcription factor by binding to PACE, a nonamer box found upstream of 26S proteasomal and other genes in yeast
TL;DR: The role of Rpn4p to function as a transregulator in yeast is corroborated by its ability of stimulating proteasome‐associated control element‐driven lacZ expression and by experiments using the RPT4 and RPT6 gene promoters coupled to the bacterial cat gene as a reporter.
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AAA proteases with catalytic sites on opposite membrane surfaces comprise a proteolytic system for the ATP-dependent degradation of inner membrane proteins in mitochondria.
Klaus Leonhard,Johannes M. Herrmann,Rosemary A. Stuart,Gertrud Mannhaupt,Walter Neupert,Thomas Langer +5 more
TL;DR: Two AAA proteases with their catalytic sites on opposite membrane surfaces constitute a novel proteolytic system for the degradation of membrane proteins in mitochondria.
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Functional analysis of 150 deletion mutants in Saccharomyces cerevisiae by a systematic approach
K. D. Entian,T. Schuster,Johannes H. Hegemann,Dietmar Becher,Horst Feldmann,Ulrich Güldener,R. Götz,M. Hansen,C. P. Hollenberg,Gregor Jansen,W. Kramer,Sabine Klein,Peter Kötter,J. Kricke,H. Launhardt,Gertrud Mannhaupt,A. Maierl,P. Meyer,W. Mewes,T. Munder,R. K. Niedenthal,M. Ramezani Rad,A. Röhmer,A. Römer,Matthias Rose,Bernd Schäfer,M.-L. Siegler,J. Vetter,N. Wilhelm,Klaus Werner Wolf,Friedrich K. Zimmermann,Alfred Zollner,Albert Hinnen +32 more
TL;DR: Surprisingly, for seven genes, additional, unexpected phenotypes were found in the authors' tests, suggesting that the type of analysis presented here provides a more complete description of gene function.
Journal ArticleDOI
Identification of a set of yeast genes coding for a novel family of putative ATPases with high similarity to constituents of the 26S protease complex.
Ralf Schnall,Gertrud Mannhaupt,Rolf Stucka,Reimund Tauer,Susanne Ehnle,Christa Schwarzlose,Irene Vetter,Horst Feldmann +7 more
TL;DR: This work has identified 12 different members of this novel gene family (the YTA family) in yeast and determined the nucleotide sequences of nine of these genes, and proposed that YTA1, Yta2, YTA3 and YTA5 function as regulatory subunits of the yeast 26S proteasome.
Journal ArticleDOI
A nuclear mutation prevents processing of a mitochondrially encoded membrane protein in Saccharomyces cerevisiae.
TL;DR: Comparison of the known DNA sequence with the partial protein sequence obtained reveals that six of the 15 residues are hydrophilic and, unlike most signal sequences, this transient sequence does not contain extended hydrophobic parts.