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Protein Science (2002), 11:2281-2284.
Copyright © 2002 The Protein Society

ACCELERATED COMMUNICATION

A CH domain-containing N terminus in NuMA?

Maria Novatchkova and Frank Eisenhaber

Research Institute of Molecular Pathology, A-1030 Vienna, Austria

Reprint requests to Frank Eisenhaber, Mail Research Institute of Molecular Pathology, Dr. Bohr-Gasse 7, A-1030 Vienna, Austria; e-mail: Frank.Eisenhaber{at}imp.univie.ac.at; fax: 43-1-7987-153.

Abstract

Nuclear mitotic apparatus protein (NuMA) is an essential vertebrate component in organizing microtubule ends at spindle poles. The NuMA-dynactin/dynein motor multiprotein complex not only explains the transport of NuMA along spindle fibers but also is linked to the process of microtubule focusing. The interaction sites of NuMA to dynein/dynactin have not been mapped. In the yet functionally uncharacterized N terminus of NuMA, we predict a calponin-homology (CH) domain, a motif with binding activity for actin-like molecules. We substantiate the primary sequence analysis-based prediction with secondary structure and fold recognition analysis, and we propose the N-terminal CH domain of NuMA as a likely interaction site for actin-related protein 1 (Arp1) protein of the dynactin/dynein complex.

Keywords: NuMA protein; mitotic spindle; nuclear matrix; calponin-homology domain; Arp1 binding; dynactin; dynein


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