Abstract
Several novel members of the kinesin superfamily, until now identified only in plants, are unique in their ability to bind calmodulin in the presence of Ca2+. Here, we identify the first such kinesin in an animal system. Sequence analysis of this new motor, called kinesin-C, predicts that it is a large carboxy-terminal kinesin, 1624 amino acid residues in length, with a predicted molecular mass of 181 kDa. Kinesin-C is predicted to contain a kinesin motor domain at its carboxy terminus, linked to a segment of alpha-helical coiled-coil 950 amino acid residues long, ending with an amino-terminal proline-rich tail domain. A putative calmodulin-binding domain resides at the extreme carboxy terminus of the motor polypeptide, and recombinant kinesin-C binds to a calmodulin-affinity column in a Ca2+-dependent fashion. The presence of this novel calmodulin-binding motor in sea urchin embryos suggests that it plays a critical role in Ca2+-dependent events during early sea urchin development.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1-8 |
| Number of pages | 8 |
| Journal | Journal of Molecular Biology |
| Volume | 294 |
| Issue number | 1 |
| DOIs | |
| State | Published - Nov 19 1999 |
| Externally published | Yes |
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Keywords
- Calmodulin
- Carboxy-terminal motor
- Kinesin
- Microtubule
- Sea urchin
ASJC Scopus subject areas
- Virology
Cite this
Identification of kinesin-C, a calmodulin-binding carboxy-terminal kinesin in animal (Strongylocentrotus purpuratus) cells. / Rogers, Gregory C.; Hart, Cynthia L.; Wedaman, Karen P.; Scholey, Jonathan M.
In: Journal of Molecular Biology, Vol. 294, No. 1, 19.11.1999, p. 1-8.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Identification of kinesin-C, a calmodulin-binding carboxy-terminal kinesin in animal (Strongylocentrotus purpuratus) cells
AU - Rogers, Gregory C.
AU - Hart, Cynthia L.
AU - Wedaman, Karen P.
AU - Scholey, Jonathan M.
PY - 1999/11/19
Y1 - 1999/11/19
N2 - Several novel members of the kinesin superfamily, until now identified only in plants, are unique in their ability to bind calmodulin in the presence of Ca2+. Here, we identify the first such kinesin in an animal system. Sequence analysis of this new motor, called kinesin-C, predicts that it is a large carboxy-terminal kinesin, 1624 amino acid residues in length, with a predicted molecular mass of 181 kDa. Kinesin-C is predicted to contain a kinesin motor domain at its carboxy terminus, linked to a segment of alpha-helical coiled-coil 950 amino acid residues long, ending with an amino-terminal proline-rich tail domain. A putative calmodulin-binding domain resides at the extreme carboxy terminus of the motor polypeptide, and recombinant kinesin-C binds to a calmodulin-affinity column in a Ca2+-dependent fashion. The presence of this novel calmodulin-binding motor in sea urchin embryos suggests that it plays a critical role in Ca2+-dependent events during early sea urchin development.
AB - Several novel members of the kinesin superfamily, until now identified only in plants, are unique in their ability to bind calmodulin in the presence of Ca2+. Here, we identify the first such kinesin in an animal system. Sequence analysis of this new motor, called kinesin-C, predicts that it is a large carboxy-terminal kinesin, 1624 amino acid residues in length, with a predicted molecular mass of 181 kDa. Kinesin-C is predicted to contain a kinesin motor domain at its carboxy terminus, linked to a segment of alpha-helical coiled-coil 950 amino acid residues long, ending with an amino-terminal proline-rich tail domain. A putative calmodulin-binding domain resides at the extreme carboxy terminus of the motor polypeptide, and recombinant kinesin-C binds to a calmodulin-affinity column in a Ca2+-dependent fashion. The presence of this novel calmodulin-binding motor in sea urchin embryos suggests that it plays a critical role in Ca2+-dependent events during early sea urchin development.
KW - Calmodulin
KW - Carboxy-terminal motor
KW - Kinesin
KW - Microtubule
KW - Sea urchin
UR - http://www.scopus.com/inward/record.url?scp=0033585135&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0033585135&partnerID=8YFLogxK
U2 - 10.1006/jmbi.1999.3249
DO - 10.1006/jmbi.1999.3249
M3 - Article
C2 - 10556023
AN - SCOPUS:0033585135
VL - 294
SP - 1
EP - 8
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 1
ER -