The 32-Kilodalton Subunit of Replication Protein A Interacts with Menin, the Product of the MEN1 Tumor Suppressor Gene

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Published inMolecular and Cellular Biology Vol. 23; no. 2; pp. 493 - 509
Main Authors Sukhodolets, Karen E., Hickman, Alison B., Agarwal, Sunita K., Sukhodolets, Maxim V., Obungu, Victor H., Novotny, Elizabeth A., Crabtree, Judy S., Chandrasekharappa, Settara C., Collins, Francis S., Spiegel, Allen M., Burns, A. Lee, Marx, Stephen J.
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.01.2003
Taylor & Francis
Subjects
Animals
Bacterial Proteins - metabolism
Blotting, Western
Cell Growth and Development
Cell Line
Cell Nucleus - metabolism
Chromatography, Gel
DNA - metabolism
DNA Damage
DNA, Complementary - metabolism
DNA-Binding Proteins - chemistry
DNA-Binding Proteins - genetics
DNA-Binding Proteins - metabolism
G1 Phase
Glutathione Transferase - metabolism
HeLa Cells
Humans
Mice
Microscopy, Fluorescence
Multiple Endocrine Neoplasia - genetics
Mutation, Missense
Neoplasm Proteins - chemistry
Neoplasm Proteins - genetics
Neoplasm Proteins - metabolism
Plasmids - metabolism
Precipitin Tests
Protein Binding
Protein Structure, Tertiary
Proto-Oncogene Proteins
Recombinant Proteins - metabolism
Replication Protein A
S Phase
Transfection
Two-Hybrid System Techniques
Online AccessGet full text

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Abstract Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to MCB .asm.org, visit: MCB       
AbstractList Menin is a 70-kDa protein encoded by MEN1, the tumor suppressor gene disrupted in multiple endocrine neoplasia type 1. In a yeast two-hybrid system based on reconstitution of Ras signaling, menin was found to interact with the 32-kDa subunit (RPA2) of replication protein A (RPA), a heterotrimeric protein required for DNA replication, recombination, and repair. The menin-RPA2 interaction was confirmed in a conventional yeast two-hybrid system and by direct interaction between purified proteins. Menin-RPA2 binding was inhibited by a number of menin missense mutations found in individuals with multiple endocrine neoplasia type 1, and the interacting regions were mapped to the N-terminal portion of menin and amino acids 43 to 171 of RPA2. This region of RPA2 contains a weak single-stranded DNA-binding domain, but menin had no detectable effect on RPA-DNA binding in vitro. Menin bound preferentially in vitro to free RPA2 rather than the RPA heterotrimer or a subcomplex consisting of RPA2 bound to the 14-kDa subunit (RPA3). However, the 70-kDa subunit (RPA1) was coprecipitated from HeLa cell extracts along with RPA2 by menin-specific antibodies, suggesting that menin binds to the RPA heterotrimer or a novel RPA1-RPA2-containing complex in vivo. This finding was consistent with the extensive overlap in the nuclear localization patterns of endogenous menin, RPA2, and RPA1 observed by immunofluorescence.
Menin is a 70-kDa protein encoded by MEN1 , the tumor suppressor gene disrupted in multiple endocrine neoplasia type 1. In a yeast two-hybrid system based on reconstitution of Ras signaling, menin was found to interact with the 32-kDa subunit (RPA2) of replication protein A (RPA), a heterotrimeric protein required for DNA replication, recombination, and repair. The menin-RPA2 interaction was confirmed in a conventional yeast two-hybrid system and by direct interaction between purified proteins. Menin-RPA2 binding was inhibited by a number of menin missense mutations found in individuals with multiple endocrine neoplasia type 1, and the interacting regions were mapped to the N-terminal portion of menin and amino acids 43 to 171 of RPA2. This region of RPA2 contains a weak single-stranded DNA-binding domain, but menin had no detectable effect on RPA-DNA binding in vitro. Menin bound preferentially in vitro to free RPA2 rather than the RPA heterotrimer or a subcomplex consisting of RPA2 bound to the 14-kDa subunit (RPA3). However, the 70-kDa subunit (RPA1) was coprecipitated from HeLa cell extracts along with RPA2 by menin-specific antibodies, suggesting that menin binds to the RPA heterotrimer or a novel RPA1-RPA2-containing complex in vivo. This finding was consistent with the extensive overlap in the nuclear localization patterns of endogenous menin, RPA2, and RPA1 observed by immunofluorescence.
Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue MCB About MCB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy MCB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0270-7306 Online ISSN: 1098-5549 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to MCB .asm.org, visit: MCB       
Author Alison B. Hickman
Stephen J. Marx
Maxim V. Sukhodolets
Francis S. Collins
Judy S. Crabtree
Allen M. Spiegel
Sunita K. Agarwal
Elizabeth A. Novotny
Victor H. Obungu
A. Lee Burns
Settara C. Chandrasekharappa
Karen E. Sukhodolets
AuthorAffiliation Metabolic Diseases Branch, National Institute of Diabetes and Digestive and Kidney Diseases, 1 Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, 2 Laboratory of Molecular Biology, National Cancer Institute, 3 Genome Technology Branch, National Human Genome Research Institute, National Institutes of Health, Bethesda, Maryland 20892 4
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/12509449$$D View this record in MEDLINE/PubMed
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Corresponding author. Mailing address: NIDDK, NIH, Bldg. 10, Rm. 9C-101, 10 Center Dr., MSC 1802, Bethesda, MD 20892-1802. Phone: (301) 402-7834. Fax: (301) 496-0200. E-mail: KarenS@intra.niddk.nih.gov.
Present address: Lilly Research Laboratories, Eli Lilly and Company, Lilly Corporate Center, Indianapolis, IN 46285.
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SSID ssj0006903
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Menin is a 70-kDa protein encoded by MEN1, the tumor suppressor gene disrupted in multiple endocrine neoplasia type 1. In a yeast two-hybrid system based on...
Menin is a 70-kDa protein encoded by MEN1 , the tumor suppressor gene disrupted in multiple endocrine neoplasia type 1. In a yeast two-hybrid system based on...
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StartPage 493
SubjectTerms Animals
Bacterial Proteins - metabolism
Blotting, Western
Cell Growth and Development
Cell Line
Cell Nucleus - metabolism
Chromatography, Gel
DNA - metabolism
DNA Damage
DNA, Complementary - metabolism
DNA-Binding Proteins - chemistry
DNA-Binding Proteins - genetics
DNA-Binding Proteins - metabolism
G1 Phase
Glutathione Transferase - metabolism
HeLa Cells
Humans
Mice
Microscopy, Fluorescence
Multiple Endocrine Neoplasia - genetics
Mutation, Missense
Neoplasm Proteins - chemistry
Neoplasm Proteins - genetics
Neoplasm Proteins - metabolism
Plasmids - metabolism
Precipitin Tests
Protein Binding
Protein Structure, Tertiary
Proto-Oncogene Proteins
Recombinant Proteins - metabolism
Replication Protein A
S Phase
Transfection
Two-Hybrid System Techniques
Title The 32-Kilodalton Subunit of Replication Protein A Interacts with Menin, the Product of the MEN1 Tumor Suppressor Gene
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https://search.proquest.com/docview/18620927
https://search.proquest.com/docview/72943444
https://pubmed.ncbi.nlm.nih.gov/PMC151531
Volume 23
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