For COVID-19 vaccine updates, please review our information guide. For patient eligibility and scheduling availability, please visit VaccineTogetherNY.org.

Disruptions of the Ustilago maydis REC2 gene identify a protein domain important in directing recombinational repair of DNA.

TitleDisruptions of the Ustilago maydis REC2 gene identify a protein domain important in directing recombinational repair of DNA.
Publication TypeJournal Article
Year of Publication2001
AuthorsKojic M, Thompson CW, Holloman WK
JournalMol Microbiol
Volume40
Issue6
Pagination1415-26
Date Published2001 Jun
ISSN0950-382X
KeywordsAmino Acid Sequence, Binding Sites, Chromosome Segregation, Diploidy, DNA Repair, Fungal Proteins, Homozygote, Meiosis, Methyl Methanesulfonate, Molecular Sequence Data, Mutagens, Mutation, Protein Structure, Tertiary, Recombinant Fusion Proteins, Recombination, Genetic, Spores, Fungal, Two-Hybrid System Techniques, Ultraviolet Rays, Ustilago, Yeasts
Abstract

The REC2 gene of Ustilago maydis encodes a homologue of the Escherichia coli RecA protein and was first identified in a screen for UV-sensitive mutants. The original isolate, rec2-1, was found to be deficient in repair of DNA damage, genetic recombination and meiosis. We report here that the rec2-197 allele, which was constructed by gene disruption, retains some biological activity and is partially dominant with respect to REC2. The basis for the residual activity is probably as a result of expression of a diffusible product from the rec2-197 allele that augments or interferes with REC2 functions. This product appears to be a polypeptide expressed from a remnant of the 5' end of the open reading frame that was not removed in creating the gene disruption. The mutator activity and disturbed meiosis of rec2-197 suggest that the Rec2 protein functions in a process that avoids spontaneous mutation and insures faithful meiotic chromosome segregation. A prediction based on the phenotype of rec2-197 is that Rec2 protein interacts with one or more other proteins in directing these functions. To identify interacting proteins we performed a yeast two-hybrid screen and found Rad51 as a candidate. Rec2-197 and Rad51 appear to interact to a similar degree.

Alternate JournalMol. Microbiol.
PubMed ID11442839
Grant ListGM42482 / GM / NIGMS NIH HHS / United States

Weill Cornell Medicine Microbiology and Immunology 1300 York Avenue, Box 62 New York, NY 10065 Phone: (212) 746-6505 Fax: (212) 746-8587