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Myung, Kyungjae
Center for Genomic Integrity
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KARP-1: A novel leucine zipper protein expressed from the Ku86 autoantigen locus is implicated in the control of DNA-dependent protein kinase activity

Author(s)
Myung, KHe, DMLee, SEHendrickson, EA
Issued Date
1997-06
DOI
10.1093/emboj/16.11.3172
URI
https://scholarworks.unist.ac.kr/handle/201301/31102
Fulltext
https://www.embopress.org/doi/10.1093/emboj/16.11.3172
Citation
EMBO JOURNAL, v.16, no.11, pp.3172 - 3184
Abstract
The Ku autoantigen plays an integral role in mammalian DNA double-strand break repair as the DNA binding component of the DNA-dependent protein kinase (DNA-PK) complex. Here, we demonstrate that a second gene, KARP-1 (Ku86 Autoantigen Related Protein-1), is expressed from the Ku86 locus. The KARP-1 gene utilizes an upstream promoter and additional exons which results in an extra 9 kDa of protein appended onto the normal Ku86 polypeptide. The KARP-1-specific domain encodes interdigitating hexa- and penta-heptad repeats of leucine residues flanked by a very basic region. Intriguingly, the catalytic subunit of DNA-PK also contains a hexa-heptad repeat of leucines. Consistent with this observation, we observed that human cell lines stably expressing dominant-negative constructs of KARP-1 resulted in diminished DNA-PK activity and X-ray hypersensitivity and that a KARP-1 antibody significantly neutralized DNA-PK activity in vitro. Finally, we present data which suggests that KARP-1 may be primate-specific. These observations have important repercussions for mammalian DNA double-strand break repair.
Publisher
WILEY
ISSN
0261-4189
Keyword (Author)
DNA-PKDNA repairKu86leucine zipper
Keyword
STRAND BREAK REPAIRIONIZING-RADIATION SENSITIVITYV(D)J RECOMBINATIONSCID MUTATIONSACCHAROMYCES-CEREVISIAEBINDING PROTEINSGENETRANSCRIPTIONSEQUENCEPROMOTER

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