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PRT1 of Arabidopsis thaliana encodes a component of the plant N-end rule pathway.

ABSTRACT: Mutants in the PRT1 gene of Arabidopsis thaliana are impaired in the degradation of a normally short-lived intracellular protein that contains a destabilizing N-terminal residue. Proteins bearing such residues are the substrates of an ubiquitin-dependent proteolytic system called the N-end rule pathway. The chromosomal position of PRT1 was determined, and the PRT1 gene was isolated by map-based cloning. The 45-kDa PRT1 protein contains two RING finger domains and one ZZ domain. No other proteins in databases match these characteristics of PRT1. There is, however, a weak similarity to Rad18p of Saccharomyces cerevisiae. The RING finger domains have been found in a number of other proteins that are involved in ubiquitin conjugation, consistent with the proposed role of PRT1 in the plant N-end rule pathway.

SUBMITTER: Potuschak T

PROVIDER: S-EPMC20902 | biostudies-literature | 1998 Jul

REPOSITORIES: biostudies-literature

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PRT1 of Arabidopsis thaliana encodes a component of the plant N-end rule pathway.

Potuschak T T Stary S S Schlögelhofer P P Becker F F Nejinskaia V V Bachmair A A

Proceedings of the National Academy of Sciences of the United States of America 19980701 14

Mutants in the PRT1 gene of Arabidopsis thaliana are impaired in the degradation of a normally short-lived intracellular protein that contains a destabilizing N-terminal residue. Proteins bearing such residues are the substrates of an ubiquitin-dependent proteolytic system called the N-end rule pathway. The chromosomal position of PRT1 was determined, and the PRT1 gene was isolated by map-based cloning. The 45-kDa PRT1 protein contains two RING finger domains and one ZZ domain. No other proteins ...[more]

PMID: 9653113

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