title: Subcellular modulation of protein VlsE stability and folding kinetics.
abstract: The interior of a cell interacts differently with proteins than a dilute buffer because of a wide variety of macromolecules, chaperones, and osmolytes that crowd and interact with polypeptide chains. We compare folding of fluorescent constructs of protein VlsE among three environments inside cells. The nucleus increases the stability of VlsE relative to the cytoplasm, but slows down folding kinetics. VlsE is also more stable in the endoplasmic reticulum, but unlike PGK, tends to aggregate there. Although fluorescent-tagged VlsE and PGK show opposite stability trends from in vitro to the cytoplasm, their trends from cytoplasm to nucleus are similar.
authors.affiliation: Department of Biochemistry, University of Illinois, Urbana, IL, USA.
authors.forename: Jonathan
authors.initials: J
authors.lastname: Tai
authors.affiliation: Center for Biophysics and Quantitative Biology, University of Illinois, Urbana, IL, USA.
authors.forename: Kapil
authors.initials: K
authors.lastname: Dave
authors.affiliation: Karlsruher Institut für Technologie, Institut für Angewandte Physik, Karlsruhe, Germany.
authors.forename: Vincent
authors.initials: V
authors.lastname: Hahn
authors.affiliation: VA New England Healthcare System, Bedford, MA, USA.
authors.forename: Irisbel
authors.initials: I
authors.lastname: Guzman
authors.affiliation: Center for Biophysics and Quantitative Biology, University of Illinois, Urbana, IL, USA.|Departments of Chemistry and Physics, University of Illinois, Urbana, IL, USA.
authors.forename: Martin
authors.initials: M
authors.lastname: Gruebele
mesh_terms: D000942:Antigens, Bacterial / Q000737:chemistry* / Q000378:metabolism; D045744:Cell Line, Tumor; D002467:Cell Nucleus / Q000378:metabolism*; D003593:Cytoplasm / Q000378:metabolism*; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D031541:Fluorescence Resonance Energy Transfer; D006801:Humans; D007700:Kinetics; D008958:Models, Molecular; D010735:Phosphoglycerate Kinase / Q000737:chemistry / Q000378:metabolism; D017510:Protein Folding; D055550:Protein Stability; D017433:Protein Structure, Secondary
chemical_list: D000942:Antigens, Bacterial; D010735:Phosphoglycerate Kinase
keywords: cellular compartments; folding kinetics; protein stability; quinary interaction