An allele of theProt locus in maize is a variant for the site of protein processing
- 1 August 1988
- journal article
- research article
- Published by Springer Nature in Biochemical Genetics
- Vol. 26 (7-8) , 463-474
- https://doi.org/10.1007/bf02399413
Abstract
An allele of theProt locus, which encodes a major globulin of the maize scutellum, is a variant for a site of protein processing. Segregation analysis and recombination mapping indicate that the variant is an allele of theProt locus. DesignatedProt-V, this allele specifies three polypeptides, V1, V2, and V3. The V1 polypeptide is incompletely processed during the proteolytic processing step catalyzed by the product of theMep locus. Cyanogen bromide cleavage studies support the precursor-product relationship between V1 and V2. The V1 product is shortened with respect to other PROT′ proteins and it is postulated that the normal site of MEP processing has been removed by this foreshortening.This publication has 8 references indexed in Scilit:
- Synthesis of Globulins in Maize EmbryosPlant Physiology, 1986
- The membrane-spanning segment of invariant chain (Iγ) contains a potentially cleavable signal sequenceCell, 1986
- Sequence interrelationships of the subunits of vicilin from pea seedsPlant Molecular Biology, 1983
- Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivityAnalytical Biochemistry, 1981
- Analysis of the size alleles of the Pro gene in maize — Evidence for a mutant protein processorMolecular Genetics and Genomics, 1979
- Identification of embryonal antigens of maize: Globulins as primary reserve proteins of the embryoPlanta, 1978
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- ALCOHOL DEHYDROGENASE POLYMORPHISM IN MAIZE—SIMPLE AND COMPOUND LOCIGenetics, 1966