In gastric chief cells, agents that activate protein kinase C (PKC) stimulate pepsinogen secretion and phosphorylation of an acidic 72-kDa protein. The isoelectric point and molecular mass of this protein are similar to those for a common PKC substrate; the MARCKS (for Myristoylated Alanine-Rich C K
Cell cycle-dependent accumulation of a kinesin-like protein, KatB/C, in synchronized tobacco BY-2 cells
โ Scribed by Hisayuki Mitsui; Seiichiro Hasezawa; Toshiyuki Nagata; Hideo Takahashi
- Publisher
- Springer
- Year
- 1996
- Tongue
- English
- Weight
- 653 KB
- Volume
- 30
- Category
- Article
- ISSN
- 0167-4412
No coin nor oath required. For personal study only.
โฆ Synopsis
Immunoblot analysis with antibodies prepared against highly purified recombinant truncated kinesin-like proteins, KatB(5-249) and KatC(207-754), encoded by the katB and katC genes of Arabidopsis thaliana revealed the presence of a kinesin-like polypeptide, termed KatB/C, in cultured tobacco BY-2 cells. The KatB/C polypeptide cosedimented with microtubules in the presence of a nonhydrolyzable ATP analogue and was released from microtubules in the presence of ATP, both of which are characteristics of kinesin proteins. The amount of KatB/C polypeptide in synchronous BY-2 cells increased during M phase of the cell cycle. Microtubule-based structures present in cells at M phase, such as the spindle and phragmoplast, may be the site of action of the KatB/C protein.
๐ SIMILAR VOLUMES