Format

Send to

Choose Destination
Comp Biochem Physiol B Biochem Mol Biol. 2014 May;171:34-41. doi: 10.1016/j.cbpb.2014.03.008. Epub 2014 Apr 12.

Two arginine kinases of Tetrahymena pyriformis: characterization and localization.

Author information

1
Laboratories of Biochemistry, Faculty of Science, Kochi University, Kochi 780-8520, Japan.
2
Cellular and Molecular Biotechnology, Faculty of Science, Kochi University, Kochi 780-8520, Japan.
3
Laboratories of Biochemistry, Faculty of Science, Kochi University, Kochi 780-8520, Japan. Electronic address: suzuki@kochi-u.ac.jp.

Abstract

Two cDNAs, one coding a typical 40-kDa arginine kinase (AK1) and the other coding a two-domain 80-kDa enzyme (AK2), were isolated from ciliate Tetrahymena pyriformis, and their recombinant enzymes were successfully expressed in Escherichia coli. Both enzymes had an activity comparable to those of typical invertebrate AKs. Interestingly, the amino acid sequence of T. pyriformis AK1, but not AK2, had a distinct myristoylation signal sequence at the N-terminus, suggesting that 40-kDa AK1 targets the membrane. Moreover, Western blot analysis showed that the AK1 is mainly localized in the ciliary fraction. Based on these results, we discuss the phosphoarginine shuttle, which enables a continuous energy flow to dynein for ciliary movement in T. pyriformis, and the role of AK1 in this model.

KEYWORDS:

Arginine kinase; Myristoylation; Phosphoarginine shuttle; Subcellular localization; Tetrahymena pyriformis

PMID:
24726623
DOI:
10.1016/j.cbpb.2014.03.008
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center