Synthesis and Localization of a Development-Specific Protein in Sclerotia of Sclerotinia sclerotiorum

Authors

Geraldine Russo, University of Nebraska-Lincoln
James L. Van Etten, University of Nebraska-LincolnFollow

Date of this Version

8-1985

Comments

Published in JOURNAL OF BACTERIOLOGY, Au. 1985, p. 696-703 0021-9193/85/080696-08$02.00/0 Copyright © 1985, American Society for Microbiology. Used by permission.

Abstract

A development-specific protein (SSP) makes up about 35 to 40% of the total protein in sclerotia of the fungus Sclerotinia sclerotiorum. The protein consists of three charge isomers, with one isomer making up 80 to 90% of the total. In vitro translation of poly(A)⁺ RNA isolated from cells in early stages of sclerotia formation revealed that 44% of the amino acids incorporated was into SSP. In vivo- and in vitro-synthesized forms of SSP migrated at identical rates on both isoelectric focusing and denaturing polyacrylamide gels, indicating that SSP was not synthesized as a larger precursor. This was significant because SSP accumulated in membrane-bound, organellelike structures which resemble protein bodies found in seeds of many higher plants.