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. 1985 Aug;163(2):696–703. doi: 10.1128/jb.163.2.696-703.1985

Synthesis and localization of a development-specific protein in sclerotia of Sclerotinia sclerotiorum.

G M Russo, J L Van Etten
PMCID: PMC219177  PMID: 2410402

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.

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Selected References

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