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A CH domain‐containing N terminus in NuMA?
Author(s) -
Novatchkova Maria,
Eisenhaber Frank
Publication year - 2002
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.0221002
Subject(s) - dynactin , dynein , microbiology and biotechnology , microtubule , calponin , multiprotein complex , spindle apparatus , biology , motor protein , chemistry , biophysics , actin , genetics , cell division , gene , cell
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.