Subcellular modulation of protein VlsE stability and folding kinetics

Jonathan Tai, Kapil Dave, Vincent Hahn, Irisbel Guzman, Martin Gruebele

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish (US)
Pages (from-to)1409-1416
Number of pages8
JournalFEBS Letters
Volume590
Issue number10
DOIs
StatePublished - May 1 2016

Keywords

  • cellular compartments
  • folding kinetics
  • protein stability
  • quinary interaction

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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