Abstract
The RAD6 gene of Saccharomyces cerevisiae encodes a ubiquitin-conjugating enzyme (E2) that is required for DNA repair, damage-induced mutagenesis, and sporulation. We have cloned the two human RAD6 homologs, designated HHR6A and HHR6B. The two 152-amino acid human proteins share 95% sequence identity with each other and approximately 70% and approximately 85% overall identity with the homologs from yeasts (S. cerevisiae and Schizosaccharomyces pombe) and Drosophila melanogaster, respectively. Neither of the human RAD6 homologs possess the acidic C-terminal sequence present in the S. cerevisiae RAD6 protein. Genetic complementation experiments reveal that HHR6A as well as HHR6B can carry out the DNA repair and mutagenesis functions of RAD6 in S. cerevisiae rad6 delta mutants.
MeSH Terms
Amino Acid Sequence
Animals
Base Sequence
DNA Probes
DNA Repair/genetics
Drosophila/genetics
Fungal Proteins/genetics
Gene Library
Genes, Fungal
Humans
Ligases/genetics
Molecular Sequence Data
Poly A/genetics,isolation & purification
RNA/genetics,isolation & purification
RNA, Messenger
Restriction Mapping
Saccharomyces cerevisiae/enzymology,genetics
Saccharomyces cerevisiae Proteins
Schizosaccharomyces/enzymology,genetics
Sequence Homology, Nucleic Acid
Ubiquitin-Conjugating Enzymes
Chemicals
DNA Probes
Fungal Proteins
RNA, Messenger
Saccharomyces cerevisiae Proteins
Poly A
RNA
RAD6 protein, S cerevisiae
UBE2A protein, human
UBE2B protein, human
Ubiquitin-Conjugating Enzymes
Ligases
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Koken M H
Department of Cell Biology and Genetics, Erasmus University, Rotterdam, The Netherlands.
Reynolds P
Jaspers-Dekker I
Prakash L
Prakash S
Bootsma D
Hoeijmakers J H
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