Structural and functional conservation of two human homologs of the yeast DNA repair gene RAD6

Marcel H.M. Koken; Paul Reynolds; Iris Jaspers-Dekker; Louise Prakash; Satya Prakash; Dirk Bootsma; Jan H.J. Hoeijmakers

doi:10.1073/pnas.88.20.8865

Structural and functional conservation of two human homologs of the yeast DNA repair gene RAD6

Marcel H.M. Koken, Paul Reynolds, Iris Jaspers-Dekker, Louise Prakash, Satya Prakash, Dirk Bootsma, Jan H.J. Hoeijmakers

Research output: Contribution to journal › Article › peer-review

247 Scopus citations

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 ≈70% and ≈85% overall identity with the homologs from yeasts (S. cerevisiae and Schizosaccharomyces pombe) and Drosophila melanogaster, respectively. Neither of the human RAD6 homologs possesses 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 rad6Δ mutants.

Original language	English (US)
Pages (from-to)	8865-8869
Number of pages	5
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	88
Issue number	20
DOIs	https://doi.org/10.1073/pnas.88.20.8865
State	Published - Oct 15 1991
Externally published	Yes

Keywords

DNA damage
E2 enzyme
Sporulation
UV mutagenesis
Ubiquitin conjugation

ASJC Scopus subject areas

General

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title = "Structural and functional conservation of two human homologs of the yeast DNA repair gene RAD6",

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 ≈70% and ≈85% overall identity with the homologs from yeasts (S. cerevisiae and Schizosaccharomyces pombe) and Drosophila melanogaster, respectively. Neither of the human RAD6 homologs possesses 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 rad6Δ mutants.",

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author = "Koken, {Marcel H.M.} and Paul Reynolds and Iris Jaspers-Dekker and Louise Prakash and Satya Prakash and Dirk Bootsma and Hoeijmakers, {Jan H.J.}",

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doi = "10.1073/pnas.88.20.8865",

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AU - Koken, Marcel H.M.

AU - Reynolds, Paul

AU - Jaspers-Dekker, Iris

AU - Prakash, Louise

AU - Prakash, Satya

AU - Bootsma, Dirk

AU - Hoeijmakers, Jan H.J.

PY - 1991/10/15

Y1 - 1991/10/15

N2 - 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 ≈70% and ≈85% overall identity with the homologs from yeasts (S. cerevisiae and Schizosaccharomyces pombe) and Drosophila melanogaster, respectively. Neither of the human RAD6 homologs possesses 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 rad6Δ mutants.

AB - 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 ≈70% and ≈85% overall identity with the homologs from yeasts (S. cerevisiae and Schizosaccharomyces pombe) and Drosophila melanogaster, respectively. Neither of the human RAD6 homologs possesses 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 rad6Δ mutants.

KW - DNA damage

KW - E2 enzyme

KW - Sporulation

KW - UV mutagenesis

KW - Ubiquitin conjugation

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Structural and functional conservation of two human homologs of the yeast DNA repair gene RAD6

Abstract

Keywords

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