Unusual properties of the fungal conventional kinesin neck domain from Neurospora crassa
AUTOR(ES)
Kallipolitou, Athina
FONTE
Oxford University Press
RESUMO
Fungal conventional kinesins are unusually fast microtubule motor proteins. To compare the functional organization of fungal and animal conventional kinesins, a set of C-terminal deletion mutants of the Neurospora crassa conventional kinesin, NcKin, was investigated for its biochemical and biophysical properties. While the shortest, monomeric construct comprising the catalytic core and the neck-linker (NcKin343) displays very high steady-state ATPase (kcat = 260/s), constructs including both the full neck and adjacent hinge domains (NcKin400, NcKin433 and NcKin480) show wild-type behaviour: they are dimeric, show fast gliding and slower ATP turnover rates (kcat = 60–84/s), and are chemically processive. Unexpectedly, a construct (NcKin378, corresponding to Drosophila KHC381) that includes just the entire coiled-coil neck is a monomer. Its ATPase activity is slow (kcat = 27/s), and chemical processivity is abolished. Together with a structural analysis of synthetic neck peptides, our data demonstrate that the NcKin neck domain behaves differently from that of animal conventional kinesins and may be tuned to drive fast, processive motility.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=125726Documentos Relacionados
- Structural comparison of dimeric Eg5, Neurospora kinesin (Nkin) and Ncd head–Nkin neck chimera with conventional kinesin
- The Neurospora organelle motor: a distant relative of conventional kinesin with unconventional properties.
- Production and Properties of Extracellular Endoxylanase from Neurospora crassa†
- The fungal H(+)-ATPase from Neurospora crassa reconstituted with fusicoccin receptors senses fusicoccin signal.
- A conserved tyrosine in the neck of a fungal kinesin regulates the catalytic motor core
