Dimerization of Human XPA and Formation of XPA2−RPA Protein Complex

Yang, Zheng-guan; Liu, Yang; Mao, Leslie Y.; Zhang, Jian-Ting; Zou, Yue

doi:10.1021/bi026064z

Cited by 70DNA Repair MechanismsProtein Structure and DynamicsEnzyme Structure and Function

Dimerization of Human XPA and Formation of XPA2−RPA Protein Complex

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Yang, Zheng-guan, Liu, Yang, Mao, Leslie Y., Zhang, Jian-Ting, Zou, Yue·2002·Biochemistry

DOI 10.1021/bi026064zPMC PMC1450105

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Abstract

XPA plays an important role in the DNA damage recognition during human nucleotide excision repair. Here we report that the XPA is a homodimer either in the free state or as a complex with human RPA in solution under normal conditions. The human XPA protein purified from baculovirus-infected sf21 insect cells has a molecular mass of 36 317 Da, as determined by mass spectroscopy. However, the apparent molecular mass of XPA determined by the native gel filtration chromatography was about 71 kDa, suggesting that XPA is a dimer. This observation was supported by a native PFO-PAGE and fluorescence spectroscopy analysis. XPA formed a dimer (XPA2) in a broad range of XPA and NaCl concentrations, and the dimerization was not due to the disulfide bond formation. Furthermore, a titration analysis of the binding of XPA to the human RPA indicated that it was the XPA2 that formed the complex with RPA. Finally, the difference between the mass spectrometric and the calculated masses of XPA implies that the protein contains posttranslational modifications. Taken together, our data suggest that the dimerization of XPA may play an important role in the DNA damage recognition of nucleotide excision repair.

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XPA, probably as a dimer, participates in DNA damage recognition and recruits other NER factors such as RPA, XPAG, and XPF/ERCC1 to the damage site to form dual incision complexes.
“XPA, likely in dimer (36), is involved in DNA damage recognition and also in the recruitment of other NER factors, such as RPA, XPAG, and XPF/ ERCC1, to the DNA damage site to form dual incision complexes through protein-protein interactions (8,10).”
From Phosphorylation of Nucleotide Excision Repair Factor Xeroderma Pigmentosum Group A by Ataxia Telangiectasia Mutated and Rad3-Related–Dependent Checkpoint Pathway Promotes Cell Survival in Response to UV Irradiation (2006) · cites this paper as [36]

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Authors: Yang, Z.-G., Liu, Y., Mao, L. Y., Zhang, J.-T., & Zou, Y.
Affiliations: East Tennessee State University (US)
Corresponding author: Zou, Yue
ORCID: Liu, Yang
Zhang, Jian-Ting
Venue: Biochemistry
Publisher: American Chemical Society (ACS)
Published: 2002-10-01
Volume: 41
Issue: 43
Pages: 13012-13020
ISSN: 0006-2960 (ISSN-L)
1520-4995
DOI: 10.1021/bi026064z
PMC: PMC1450105
OpenAlex: W2054183087
Cited by: 70
References: 39
Citations by year: 2026: 1 · 2024: 2 · 2023: 2 · 2022: 2 · 2020: 3 · 2019: 1 · 2018: 2 · 2017: 2 · 2016: 4 · 2015: 2 · 2014: 3 · 2012: 4
FWCI: 1.62
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Biochemistry (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
IUScholarWorks (Indiana University) (submittedVersion)
Digital Commons - East Tennessee State University (East Tennessee State University) (submittedVersion)
Funders: National Cancer Institute (R56CA086927, CA-64539, R01CA086927, CA-86927)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Keywords: XPA, homodimerization, RPA, nucleotide excision repair, DNA damage recognition, protein-protein complex formation, post-translational modification, protein molecular weight
MeSH terms: Animals, Caprylates, Chromatography, Gel, DNA Repair, DNA Replication, DNA-Binding Proteins, Electrophoresis, Polyacrylamide Gel, Escherichia coli, Fluorocarbons, Humans, Molecular Weight, Protein Binding, Protein Processing, Post-Translational, Recombinant Proteins, Spectrometry, Fluorescence, Spodoptera, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Dimerization, Macromolecular Substances, Replication Protein A, Xeroderma Pigmentosum Group A Protein

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Dimerization of Human XPA and Formation of XPA2−RPA Protein Complex

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