Synthesis and localization of a development-specific protein in sclerotia of Sclerotinia sclerotiorum.
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.
Russo
G M
GM
Van Etten
J L
JL
D001203:Ascomycota / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D004591:Electrophoresis, Polyacrylamide Gel; D005656:Fungal Proteins / Q000096:biosynthesis* / Q000235:genetics / Q000302:isolation & purification; D007536:Isomerism; D007700:Kinetics; D008854:Microscopy, Electron; D011061:Poly A / Q000235:genetics; D011132:Polyribosomes / Q000378:metabolism; D014176:Protein Biosynthesis; D012313:RNA / Q000235:genetics; D012333:RNA, Messenger / Q000235:genetics
D005656:Fungal Proteins; D012333:RNA, Messenger; C046132:development-specific protein (Sclerotinia); D011061:Poly A; D012313:RNA