Kinesin subfamily UNC104 contains a FHA domain: boundaries and physicochemical characterization.

Abstract:

:By sequence analysis we show that the U104 domain found in the UNC104 subfamily of kinesins is a forkhead homology-associated domain (FHA). A combination of limited proteolysis, mass spectroscopy, and physicochemical analysis define this domain as a genuine autonomously folding domain. Our data show that the FHA domain is shorter than previously reported since the C-terminal alpha-helix is not part of its minimum core. Key amino acids postulated to recognize phosphorylated residues are conserved. These data suggest that the kinesin FHA domains are functional domains involved in protein-protein interactions regulated by phosphorylation.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Westerholm-Parvinen A,Vernos I,Serrano L

doi

10.1016/s0014-5793(00)02310-3

keywords:

subject

Has Abstract

pub_date

2000-12-15 00:00:00

pages

285-90

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(00)02310-3

journal_volume

486

pub_type

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