Isolation and analysis of a cDNA clone encoding an S. guttatum alternataive oxidase protein

Conference · Tue May 01 04:00:00 EDT 1990 · Plant Physiology, Supplement; (USA)

OSTI ID:5627959

Rhoads, D M; McIntosh, L ^[1]

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1. MSU-DOE Plant Research Laboratory, East Lansing, MI (USA) Michigan State Univ., East Lansing (USA)

Antibodies that recognize the 35, 36, and 37 kilodalton (kDa) alternative oxidase proteins were used to isolate a cDNA proteins were used to isolate a cDNA clone of a nuclearly encoded protein of Sauromatum guttatum. The amino acid sequence deduced from clone pAOSG81 revealed a protein with a predicted molecular mass of 44 kDa, while a 42 kDa protein is immunoprecipitated from in vitro translation products made using S. guttatum poly A+ RNA. The protein contains a 60-65 amino acid transit peptide which is predicted to form amphiphilic helices. We have also identified regions of the mature 42 kDa protein which are likely to be membrane associated. Clone pAOSG81 is being used to screen a genomic library. The genomic clone encoding the 42 kDa protein will be used to investigate the salicylic-acid-controlled transcriptional regulation of the S. guttatum alternative oxidase proteins.

• OSTI ID: 5627959
• Report Number(s): CONF-9007196--
• Conference Information: Journal Name: Plant Physiology, Supplement; (USA) Journal Volume: 93:1
• Country of Publication: United States
• Language: English

Related Subjects

550400* -- Genetics
59 BASIC BIOLOGICAL SCIENCES
ANTIBODIES
CARBOXYLIC ACIDS
CLONING
DNA
DNA HYBRIDIZATION
DNA-CLONING
ENZYMES
HERBS
HYBRIDIZATION
HYDROXY ACIDS
NUCLEIC ACIDS
ORGANIC ACIDS
ORGANIC COMPOUNDS
OXIDOREDUCTASES
PLANTS
PROTEIN STRUCTURE
SALICYLIC ACID