Mutational analysis of the structure and function of the xeroderma pigmentosum group A complementing protein. Identification of essential domains for nuclear localization and DNA excision repair.
Open accessAbstract
We showed previously that the xeroderma pigmentosum group A complementing (XPAC) protein involved in the DNA excision repair pathway contains a zinc-finger motif and is localized in the nucleus of normal human cells. For detailed structural and functional analyses of the XPAC protein, we constructed various XPAC cDNAs by site-directed mutagenesis and isolated permanent cell lines expressing mutant proteins. Immunofluorescent analysis of these lines indicated that the nuclear localization signal is located in the region encoded by Exon 1, especially centered at amino acids 30-42. A UV survival study showed that regions from Exons 2 through 6 were essential for DNA repair function, but that Exon 1 was not. Interestingly, deletion of the glutamic acid cluster in the region encoded by Exon 2 resulted in a dramatic loss of DNA repair activity. Furthermore, replacements of each of the 4 cysteines supposed to form a zinc-finger structure in the region encoded by Exon 3 by serine or glycine resulted in similar levels of loss of repair activity. These results suggest that all 4 cysteines forming a zinc-finger structure and also the glutamic acid cluster are important for DNA repair function.
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XPA's nuclear localization sequence contains basic residues at positions 30-34 of the 273-amino-acid protein.
“The targeting of XPA to the nucleus occurs via its nuclear localization sequence (NLS) which contains basic residues located at positons 30–34 of the 273 amino acid protein 62, 63, 82, 68.”
From Xeroderma Pigmentosa Group A (XPA), Nucleotide Excision Repair and Regulation by ATR in Response to Ultraviolet Irradiation (2017) · cites this paper as [63]
A NLS-like motif -RKRQR- is located in the N-terminus of XPA (residues 30-34).
“Among these domains, a NLS-like motif -RKRQR-) is located in the N-terminus (residues 30–34) [38]”
From UV-Induced Nuclear Import of XPA Is Mediated by Importin-α4 in An ATR-Dependent Manner (2013) · cites this paper as [38]
Formaldehyde rather than methanol was employed in the reports of a nucleus-only location for XPA.
“Formaldehyde rather than methanol was employed in the reports of a nucleus-only location for XPA [38], [51], [52].”
From UV-Induced Nuclear Import of XPA Is Mediated by Importin-α4 in An ATR-Dependent Manner (2013) · cites this paper as [38]
Reports of immunofluorescence microscopic analyses showed that XPA was fully localized to the nucleus even in the absence of DNA damage.
“reports of immunofluorescence microscopic analyses that showed that XPA was fully localized to the nucleus even in the absence of DNA damage [38], [51], [52].”
From UV-Induced Nuclear Import of XPA Is Mediated by Importin-α4 in An ATR-Dependent Manner (2013) · cites this paper as [38]
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- Authors
- Miyamoto, I., Miura, N., Niwa, H., Miyazaki, J., & Tanaka, K.
- Affiliations
- Hyogo Medical University (JP)
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1992-06
- Volume
- 267
- Issue
- 17
- Pages
- 12182-12187
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2127547755
- Cited by
- 122
- References
- 25
- Citations by year
- 2026: 1 · 2023: 1 · 2022: 2 · 2021: 1 · 2020: 1 · 2018: 1 · 2017: 4 · 2016: 4 · 2015: 1 · 2014: 2 · 2013: 4 · 2012: 1
- FWCI
- 2.91
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- excision repair, nucleotide excision repair, zinc finger, nuclear localization signal, cysteine residues, site-directed mutagenesis, UV-induced DNA damage, protein structure-function relationship
- MeSH terms
- Amino Acid Sequence, Base Sequence, Cell Line, Cell Nucleus, DNA, DNA Repair, DNA-Binding Proteins, Escherichia coli, Fluorescent Antibody Technique, Humans, Molecular Sequence Data, Recombinant Proteins, Structure-Activity Relationship, Transfection, Xeroderma Pigmentosum, Mutagenesis, Site-Directed, Zinc Fingers, Xeroderma Pigmentosum Group A Protein
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