Role of methionine-1 in ubiquitin conformation and activity Academic Article Article uri icon

Overview

MeSH Major

  • Carrier Proteins
  • Cell Membrane
  • Endoplasmic Reticulum
  • Mitochondrial Proteins
  • Saccharomyces cerevisiae Proteins
  • Sterols

abstract

  • Methionine-1 of ubiquitin was oxidized to the sulfone without significant effect on biological activity or conformation at neutral pH. However, at low pH, the oxidized protein expanded to a more open conformation, similar in gel sieving properties to denatured ubiquitin but similar in secondary structure to native ubiquitin. This conformational transition was absent in the native protein. Interpretation of these results in the light of X-ray data suggests that ubiquitin contains two independently folded domains that are held together in part by a hydrogen bond between Met-1 and Lys-63 and which can be separated when this bond is broken. It is suggested that separation of these domains may occur upon ubiquitin conjugation.

publication date

  • July 16, 1986

Research

keywords

  • Academic Article

Identity

Digital Object Identifier (DOI)

  • 10.1016/0006-291X(86)90300-1

PubMed ID

  • 3017328

Additional Document Info

start page

  • 437

end page

  • 44

volume

  • 138

number

  • 1