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Title: Characterization of hampin/MSL1 as a node in the nuclear interactome

Abstract

Hampin, homolog of Drosophila MSL1, is a partner of histone acetyltransferase MYST1/MOF. Functions of these proteins remain poorly understood beyond their participation in chromatin remodeling complex MSL. In order to identify new proteins interacting with hampin, we screened a mouse cDNA library in yeast two-hybrid system with mouse hampin as bait and found five high-confidence interactors: MYST1, TPR proteins TTC4 and KIAA0103, NOP17 (homolog of a yeast nucleolar protein), and transcription factor GC BP. Subsequently, all these proteins were used as baits in library screenings and more new interactions were found: tumor suppressor RASSF1C and spliceosome component PRP3 for KIAA0103, ring finger RNF10 for RASSF1C, and RNA polymerase II regulator NELF-C for MYST1. The majority of the observed interactions was confirmed in vitro by pull-down of bacterially expressed proteins. Reconstruction of a fragment of mammalian interactome suggests that hampin may be linked to diverse regulatory processes in the nucleus.

Authors:
 [1];  [1];  [2];  [1];  [1];  [3];  [1];  [2];
  1. Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997 (Russian Federation)
  2. (United States)
  3. Department of Physiology, Pharmacology, Metabolism, and Cardiovascular Sciences, University of Toledo College of Medicine, Toledo, OH 43614 (United States)
Publication Date:
OSTI Identifier:
20979889
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 355; Journal Issue: 4; Other Information: DOI: 10.1016/j.bbrc.2007.02.073; PII: S0006-291X(07)00363-4; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; CHROMATIN; DROSOPHILA; HYBRID SYSTEMS; IN VITRO; MICE; NEOPLASMS; NITRIC OXIDE; PHOSPHATES; RNA POLYMERASES; TRANSCRIPTION FACTORS; YEASTS

Citation Formats

Dmitriev, Ruslan I., Korneenko, Tatyana V., Department of Physiology, Pharmacology, Metabolism, and Cardiovascular Sciences, University of Toledo College of Medicine, Toledo, OH 43614, Bessonov, Alexander A., Shakhparonov, Mikhail I., Modyanov, Nikolai N., Pestov, Nikolay B., Department of Physiology, Pharmacology, Metabolism, and Cardiovascular Sciences, University of Toledo College of Medicine, Toledo, OH 43614, and E-mail: korn@mail.ibch.ru. Characterization of hampin/MSL1 as a node in the nuclear interactome. United States: N. p., 2007. Web. doi:10.1016/j.bbrc.2007.02.073.
Dmitriev, Ruslan I., Korneenko, Tatyana V., Department of Physiology, Pharmacology, Metabolism, and Cardiovascular Sciences, University of Toledo College of Medicine, Toledo, OH 43614, Bessonov, Alexander A., Shakhparonov, Mikhail I., Modyanov, Nikolai N., Pestov, Nikolay B., Department of Physiology, Pharmacology, Metabolism, and Cardiovascular Sciences, University of Toledo College of Medicine, Toledo, OH 43614, & E-mail: korn@mail.ibch.ru. Characterization of hampin/MSL1 as a node in the nuclear interactome. United States. doi:10.1016/j.bbrc.2007.02.073.
Dmitriev, Ruslan I., Korneenko, Tatyana V., Department of Physiology, Pharmacology, Metabolism, and Cardiovascular Sciences, University of Toledo College of Medicine, Toledo, OH 43614, Bessonov, Alexander A., Shakhparonov, Mikhail I., Modyanov, Nikolai N., Pestov, Nikolay B., Department of Physiology, Pharmacology, Metabolism, and Cardiovascular Sciences, University of Toledo College of Medicine, Toledo, OH 43614, and E-mail: korn@mail.ibch.ru. Fri . "Characterization of hampin/MSL1 as a node in the nuclear interactome". United States. doi:10.1016/j.bbrc.2007.02.073.
@article{osti_20979889,
title = {Characterization of hampin/MSL1 as a node in the nuclear interactome},
author = {Dmitriev, Ruslan I. and Korneenko, Tatyana V. and Department of Physiology, Pharmacology, Metabolism, and Cardiovascular Sciences, University of Toledo College of Medicine, Toledo, OH 43614 and Bessonov, Alexander A. and Shakhparonov, Mikhail I. and Modyanov, Nikolai N. and Pestov, Nikolay B. and Department of Physiology, Pharmacology, Metabolism, and Cardiovascular Sciences, University of Toledo College of Medicine, Toledo, OH 43614 and E-mail: korn@mail.ibch.ru},
abstractNote = {Hampin, homolog of Drosophila MSL1, is a partner of histone acetyltransferase MYST1/MOF. Functions of these proteins remain poorly understood beyond their participation in chromatin remodeling complex MSL. In order to identify new proteins interacting with hampin, we screened a mouse cDNA library in yeast two-hybrid system with mouse hampin as bait and found five high-confidence interactors: MYST1, TPR proteins TTC4 and KIAA0103, NOP17 (homolog of a yeast nucleolar protein), and transcription factor GC BP. Subsequently, all these proteins were used as baits in library screenings and more new interactions were found: tumor suppressor RASSF1C and spliceosome component PRP3 for KIAA0103, ring finger RNF10 for RASSF1C, and RNA polymerase II regulator NELF-C for MYST1. The majority of the observed interactions was confirmed in vitro by pull-down of bacterially expressed proteins. Reconstruction of a fragment of mammalian interactome suggests that hampin may be linked to diverse regulatory processes in the nucleus.},
doi = {10.1016/j.bbrc.2007.02.073},
journal = {Biochemical and Biophysical Research Communications},
number = 4,
volume = 355,
place = {United States},
year = {Fri Apr 20 00:00:00 EDT 2007},
month = {Fri Apr 20 00:00:00 EDT 2007}
}
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