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Title: Malate synthase a membrane protein

Conference · · Plant Physiol., Suppl.; (United States)
OSTI ID:6073154

Malate synthase (MS) is generally regarded as a peripheral membrane protein, and believed by some to be ontogenetically associated with ER. However, immuno- and cyto-chemical in situ localizations show MS throughout the matrix of cotton (and cucumber) glyoxysomes, not specifically near their boundary membranes, nor in ER. Only a maximum of 50% MS can be solubilized from cotton glyoxysomes with 1% Triton X-100, 2mM Zwittergen 14, or 10mM DOC +/- salts. Cotton MS does not incorporate /sup 3/H-glucosamine in vivo, nor does it react with Con A on columns or blots. Cotton MS banded with ER in sucrose gradients (20-40%) in Tricine after 3h, but not after 22h in Tricine or Hepes, or after 3h in Hepes or K-phosphate. Collectively the authors data are inconsistent with physiologically meaningful MS-membrane associations in ER or glyoxysomes. It appears that experimentally-induced aggregates of MS migrate in ER gradients and occur in isolated glyoxysomes. These data indicate that ER is not involved in synthesis or modification of cottonseed MS prior to its import into the glyoxysomal matrix.

Research Organization:
Arizona State Univ., Tempe
OSTI ID:
6073154
Report Number(s):
CONF-8707108-; TRN: 87-037216
Journal Information:
Plant Physiol., Suppl.; (United States), Vol. 83:4; Conference: Annual meeting of the American Society of Plant Physiologists, St. Louis, MO, USA, 19 Jul 1987
Country of Publication:
United States
Language:
English