A novel kinesin-like protein with a calmodulin-binding domain

W Wang; D Takezawa; S B Narasimhulu; A S Reddy; B W Poovaiah

doi:10.1007/BF00020609

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A novel kinesin-like protein with a calmodulin-binding domain

Journal article

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Peer reviewed

A novel kinesin-like protein with a calmodulin-binding domain

W Wang, D Takezawa, S B Narasimhulu, A S Reddy and B W Poovaiah

Plant molecular biology, Vol.31(1), pp.87-100

04/1996

DOI: https://doi.org/10.1007/BF00020609

Handle:

https://hdl.handle.net/2376/113507

PMID: 8704162

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Abstract

Calmodulin-Binding Proteins - genetics

Amino Acid Sequence

Calmodulin - metabolism

Protein Structure, Secondary

Calcium - metabolism

Adenosine Triphosphatases - metabolism

Molecular Sequence Data

Calmodulin-Binding Proteins - chemistry

Calmodulin-Binding Proteins - metabolism

Kinesin - metabolism

Sequence Homology, Amino Acid

Plant Proteins - genetics

Animals

Escherichia coli - genetics

Plant Proteins - chemistry

Tobacco - genetics

Base Sequence

Kinesin - genetics

Protein Binding

Plant Proteins - metabolism

DNA, Complementary

Plants, Toxic

Calcium regulates diverse developmental processes in plants through the action of calmodulin. A cDNA expression library from developing anthers of tobacco was screened with 35S-labeled calmodulin to isolate cDNAs encoding calmodulin-binding proteins. Among several clones isolated, a kinesin-like gene (TCK1) that encodes a calmodulin-binding kinesin-like protein was obtained. The TCK1 cDNA encodes a protein with 1265 amino acid residues. Its structural features are very similar to those of known kinesin heavy chains and kinesin-like proteins from plants and animals, with one distinct exception. Unlike other known kinesin-like proteins, TCK1 contains a calmodulin-binding domain which distinguishes it from all other known kinesin genes. Escherichia coli-expressed TCK1 binds calmodulin in a Ca(2+)-dependent manner. In addition to the presence of a calmodulin-binding domain at the carboxyl terminal, it also has a leucine zipper motif in the stalk region. The amino acid sequence at the carboxyl terminal of TCK1 has striking homology with the mechanochemical motor domain of kinesins. The motor domain has ATPase activity that is stimulated by microtubules. Southern blot analysis revealed that TCK1 is coded by a single gene. Expression studies indicated that TCK1 is expressed in all of the tissues tested. Its expression is highest in the stigma and anther, especially during the early stages of anther development. Our results suggest that Ca2+/calmodulin may play an important role in the function of this microtubule-associated motor protein and may be involved in the regulation of microtubule-based intracellular transport.

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Title: A novel kinesin-like protein with a calmodulin-binding domain
Creators: W Wang - Department of Horticulture, Washington State University, Pullman 99164-6414, USA
D Takezawa
S B Narasimhulu
A S Reddy
B W Poovaiah
Publication Details: Plant molecular biology, Vol.31(1), pp.87-100
Academic Unit: Department of Horticulture
Publisher: Netherlands
Identifiers: 99900547927201842
Language: English
Resource Type: Journal article