Truncated staphylococcal nuclease is compact but disordered

John M. Flanagan, Mikio Kataoka, David Shortle, Donald M. Engelman

Research output: Contribution to journalArticlepeer-review

Abstract

Deletion of 13 amino acids from the carboxyl terminus of the 149-amino acid staphylococcal nuclease molecule results in a denatured, partly unfolded molecule that lacks persistent secondary structure but is compact under physiological conditions. Since the modification is a carboxyl-terminal deletion, it is argued that the state resembles a peptide emerging from the ribosome just before the complete folding pathway is initiated. In this paper, we characterize the molecule by nuclear magnetic resonance, circular dichroism, and small-angle x-ray scattering measurements. The truncated nuclease shows wild-type levels of activity in the presence of calcium and is found to fold into a native-like conformation in the presence of 3′,5′-bisphospho-2′-deoxythymidine, a potent inhibitor. Thus, the truncated molecule retains the capacity to fold. Our results suggest that extensive solvent exclusion generates a compact polypeptide chain prior to the development of persistent secondary structural features as a protein folds during biosynthesis.

Original languageEnglish (US)
Pages (from-to)748-752
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume89
Issue number2
DOIs
StatePublished - 1992

Keywords

  • Folding
  • Polypeptide

ASJC Scopus subject areas

  • General

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