Characterization of a wide range base-damage-endonuclease activity of mammalian rpS3

Sang Hwa Kim; Jae Yung Lee; Joon Kim

doi:10.1016/j.bbrc.2005.01.045

Characterization of a wide range base-damage-endonuclease activity of mammalian rpS3

Sang Hwa Kim, Jae Yung Lee, Joon Kim

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

54 Citations (Scopus)

Abstract

Mammalian rpS3, a ribosomal protein S3 with a DNA repair endonuclease activity, nicks heavily UV-irradiated DNA and DNA containing AP sites. RpS3 calls for a novel endonucleolytic activity on AP sites generated from pyrimidine dimers by T4 pyrimidine dimer glycosylase activity. This study revealed that rpS3 cleaves the lesions including AP sites, thymine glycols, and other UV damaged lesions such as pyrimidine dimers. This enzyme does not have a glycosylase activity as predicted from its amino acid sequence. However, it has an endonuclease activity on DNA containing thymine glycol, which is exactly overlapped with UV-irradiated or AP DNAs, indicating that rpS3 cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity acting as a base-damage-endonuclease. RpS3 cleaves supercoiled UV damaged DNA more efficiently than the relaxed counterpart, and the endonuclease activity of rpS3 was inhibited by MgCl₂ on AP DNA but not on UV-irradiated DNA.

Original language	English
Pages (from-to)	962-967
Number of pages	6
Journal	Biochemical and biophysical research communications
Volume	328
Issue number	4
DOIs	https://doi.org/10.1016/j.bbrc.2005.01.045
Publication status	Published - 2005 Mar 25

Bibliographical note

Funding Information:
We are deeply indebted to Dr. Stuart Linn at U.C. Berkeley for helpful discussion and this work was supported in part by KRF Grant C00073.

Keywords

AP
DNA repair
UV endonuclease
rpS3

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2005.01.045

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title = "Characterization of a wide range base-damage-endonuclease activity of mammalian rpS3",

abstract = "Mammalian rpS3, a ribosomal protein S3 with a DNA repair endonuclease activity, nicks heavily UV-irradiated DNA and DNA containing AP sites. RpS3 calls for a novel endonucleolytic activity on AP sites generated from pyrimidine dimers by T4 pyrimidine dimer glycosylase activity. This study revealed that rpS3 cleaves the lesions including AP sites, thymine glycols, and other UV damaged lesions such as pyrimidine dimers. This enzyme does not have a glycosylase activity as predicted from its amino acid sequence. However, it has an endonuclease activity on DNA containing thymine glycol, which is exactly overlapped with UV-irradiated or AP DNAs, indicating that rpS3 cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity acting as a base-damage-endonuclease. RpS3 cleaves supercoiled UV damaged DNA more efficiently than the relaxed counterpart, and the endonuclease activity of rpS3 was inhibited by MgCl2 on AP DNA but not on UV-irradiated DNA.",

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author = "Kim, {Sang Hwa} and Lee, {Jae Yung} and Joon Kim",

note = "Funding Information: We are deeply indebted to Dr. Stuart Linn at U.C. Berkeley for helpful discussion and this work was supported in part by KRF Grant C00073.",

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AU - Kim, Sang Hwa

AU - Lee, Jae Yung

AU - Kim, Joon

N1 - Funding Information: We are deeply indebted to Dr. Stuart Linn at U.C. Berkeley for helpful discussion and this work was supported in part by KRF Grant C00073.

PY - 2005/3/25

Y1 - 2005/3/25

N2 - Mammalian rpS3, a ribosomal protein S3 with a DNA repair endonuclease activity, nicks heavily UV-irradiated DNA and DNA containing AP sites. RpS3 calls for a novel endonucleolytic activity on AP sites generated from pyrimidine dimers by T4 pyrimidine dimer glycosylase activity. This study revealed that rpS3 cleaves the lesions including AP sites, thymine glycols, and other UV damaged lesions such as pyrimidine dimers. This enzyme does not have a glycosylase activity as predicted from its amino acid sequence. However, it has an endonuclease activity on DNA containing thymine glycol, which is exactly overlapped with UV-irradiated or AP DNAs, indicating that rpS3 cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity acting as a base-damage-endonuclease. RpS3 cleaves supercoiled UV damaged DNA more efficiently than the relaxed counterpart, and the endonuclease activity of rpS3 was inhibited by MgCl2 on AP DNA but not on UV-irradiated DNA.

AB - Mammalian rpS3, a ribosomal protein S3 with a DNA repair endonuclease activity, nicks heavily UV-irradiated DNA and DNA containing AP sites. RpS3 calls for a novel endonucleolytic activity on AP sites generated from pyrimidine dimers by T4 pyrimidine dimer glycosylase activity. This study revealed that rpS3 cleaves the lesions including AP sites, thymine glycols, and other UV damaged lesions such as pyrimidine dimers. This enzyme does not have a glycosylase activity as predicted from its amino acid sequence. However, it has an endonuclease activity on DNA containing thymine glycol, which is exactly overlapped with UV-irradiated or AP DNAs, indicating that rpS3 cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity acting as a base-damage-endonuclease. RpS3 cleaves supercoiled UV damaged DNA more efficiently than the relaxed counterpart, and the endonuclease activity of rpS3 was inhibited by MgCl2 on AP DNA but not on UV-irradiated DNA.

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Characterization of a wide range base-damage-endonuclease activity of mammalian rpS3

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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