title: Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function.
abstract: Hsp12 of S. cerevisiae is upregulated several 100-fold in response to stress. Our phenotypic analysis showed that this protein is important for survival of a variety of stress conditions, including high temperature. In the absence of Hsp12, we observed changes in cell morphology under stress conditions. Surprisingly, in the cell, Hsp12 exists both as a soluble cytosolic protein and associated to the plasma membrane. The in vitro analysis revealed that Hsp12, unlike all other Hsps studied so far, is completely unfolded; however, in the presence of certain lipids, it adopts a helical structure. The presence of Hsp12 does not alter the overall lipid composition of the plasma membrane but increases membrane stability.
authors.affiliation: Munich Center for Integrated Protein Science, Technische Universität München, Department Chemie, Lichtenbergstrasse 4, 85747 Garching, Germany.
authors.forename: Sylvia
authors.initials: S
authors.lastname: Welker
authors.forename: Birgit
authors.initials: B
authors.lastname: Rudolph
authors.forename: Elke
authors.initials: E
authors.lastname: Frenzel
authors.forename: Franz
authors.initials: F
authors.lastname: Hagn
authors.forename: Gerhard
authors.initials: G
authors.lastname: Liebisch
authors.forename: Gerd
authors.initials: G
authors.lastname: Schmitz
authors.forename: Johannes
authors.initials: J
authors.lastname: Scheuring
authors.forename: Andreas
authors.initials: A
authors.lastname: Kerth
authors.forename: Alfred
authors.initials: A
authors.lastname: Blume
authors.forename: Sevil
authors.initials: S
authors.lastname: Weinkauf
authors.forename: Martin
authors.initials: M
authors.lastname: Haslbeck
authors.forename: Horst
authors.initials: H
authors.lastname: Kessler
authors.forename: Johannes
authors.initials: J
authors.lastname: Buchner
mesh_terms: D002462:Cell Membrane / Q000378:metabolism* / Q000648:ultrastructure; D003600:Cytosol / Q000378:metabolism; D015966:Gene Expression Regulation, Fungal; D005838:Genotype; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D018869:Heat-Shock Response; D008560:Membrane Fluidity; D008563:Membrane Lipids / Q000378:metabolism; D009997:Osmotic Pressure; D018384:Oxidative Stress; D010641:Phenotype; D017510:Protein Folding; D017433:Protein Structure, Secondary; D021381:Protein Transport; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000254:growth & development / Q000378:metabolism* / Q000648:ultrastructure; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D017384:Sequence Deletion; D013312:Stress, Physiological; D013329:Structure-Activity Relationship
chemical_list: C112591:HSP12 protein, S cerevisiae; D006360:Heat-Shock Proteins; D008563:Membrane Lipids; D029701:Saccharomyces cerevisiae Proteins