(Processing and targeting of the thiol protease aleurain)

Technical Report · Mon Jan 01 00:00:00 EST 1990

DOI:https://doi.org/10.2172/6995327· OSTI ID:6995327

Rogers, J C

Our goal for work during the past two years under this Grant was to characterize the barley thiol protease, aleurain, to determine if it is secreted or retained intracellularly in aleurone cells, and to begin to elucidate structural features that might control targeting of the protein to its final destination. We have shown that aleurain is synthesized as a proenzyme with two N-linked oligosaccharide chains, one high mannose-type and one complex-type. Aleurain undergoes processing to mature form by removal of an Nterminal prosegment, and is retained intracellularly; it cannot be detected among proteins secreted from aleurone cells. Treatment of aleurone cells with tunicamycin to prevent glycosylation of aleurain does not prevent processing of the unglycosylated form. The N-terminal portion of aleurain's prosegment is homologous to the comparable region in two yeast vacuolar proteases, where that region is known to contain the signal necessary for targeting the proteases to the vacuole. 18 refs., 7 figs.

• Research Organization: Washington Univ., St. Louis, MO (USA). Dept. of Hematology and Oncology
• Sponsoring Organization: DOE/ER
• DOE Contract Number: FG02-87ER13704
• OSTI ID: 6995327
• Report Number(s): DOE/ER/13704-3; ON: DE90009522
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
PROTEINS
GENETIC CONTROL
SH-PROTEINASES
DNA SEQUENCING
BARLEY
DECAY
GENE REGULATION
GENETIC ENGINEERING
PLANTS
PROGRESS REPORT
RECOMBINANT DNA
RNA PROCESSING
CEREALS
CONTROL
DNA
DOCUMENT TYPES
ENZYMES
GRASS
HYDROLASES
LILIOPSIDA
MAGNOLIOPHYTA
NUCLEIC ACIDS
ORGANIC COMPOUNDS
PEPTIDE HYDROLASES
PEST CONTROL
STRUCTURAL CHEMICAL ANALYSIS
550200* - Biochemistry
550400 - Genetics