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

AUTOR(ES)

Potuschak, Thomas

FONTE

The National Academy of Sciences

RESUMO

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.

Documentos Relacionados

• PRT1 of Arabidopsis Is a Ubiquitin Protein Ligase of the Plant N-End Rule Pathway with Specificity for Aromatic Amino-Terminal Residues1
• The recognition component of the N-end rule pathway.
• Inhibition of the N-end rule pathway in living cells.
• The mouse and human genes encoding the recognition component of the N-end rule pathway
• The N-end rule: functions, mysteries, uses.