Skip Navigation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Takagi, T.
Right arrow Articles by Nakamura, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Takagi, T.
Right arrow Articles by Nakamura, A.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1993, Vol. 113, No. 3 321-326
© 1993 Japanese Biochemical Society

research-article

Structure of 29-kDa Protein from Ascidian(Halocynthia roretzi) Body Wall Muscle1

Takashi Takagi, Hideaki Yasunaga and Akio Nakamura3

Biological Institute, Faculty of Science, Tohoku University Aoba-ku, Sendai, Miyagi 980

Preparations of thin filament from ascidian (Halocynthia roretzi) body wall muscle were found to be contaminated with large amounts of an unknown protein which, when purified, migrated to 29 kDa on SDS-PAGE and was thus named HR-29. To elucidate its physiological function, we have determined the primary structure of HR-29 by peptide and cDNA sequence analysis. Genomic sequence analysis showed that HR-29 is divided to four exons by three introns. It is composed of 251 amino acid residues and the N-terminal Ser is blocked by an acetyl group. The N-terminal domain of 150 residues is hydrophilic, and from residue 36 to 92 there are three similar repeated sequences of 19 residues. The N-terminal domain showed no significant sequence homology with other proteins. On the other hand, the C-terminal domain of 100 residues has homology with those of small heat-shock proteins and a-crystallin of lens protein. HR-29 is thought to be a fusion protein of two different origins. Recently aB-crystallin was identified in skeletal muscle and suggested to be a myofibril-stabilizing protein [Atoml, T. et al. (1991) J. Biochem. 110, 2360-2364]. Thus, HR-29 may also be a myofibril-stabilizing protein, as suggested by the sequence similarity of the C-terminal domain with a-crystallin, although the origin and role of the N-terminal domain are not clear.

1The nucleotide sequences reported in this paper will appear in the DDBJ, EMBL, and GenBank Nucleotide Sequence Databases with accession numbers D13917 [GenBank] (Halocynthia roretzi DNA for HR-29).

2Kobayashi Pharmaceutical Co., Ltd., Yodogawaku, Osaka 582;

3Department of Pharmacology, Gunma University School of Medicine Maebashi, Gunma371


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Physiol. Rev.Home page
S. L. Hooper and J. B. Thuma
Invertebrate Muscles: Muscle Specific Genes and Proteins
Physiol Rev, July 1, 2005; 85(3): 1001 - 1060.
[Abstract] [Full Text] [PDF]

Home page
 Genes Dev.Home page
A. E. Vandenberghe, T. H. Meedel, and K. E.M. Hastings
mRNA 5'-leader trans-splicing in the chordates
Genes & Dev., February 1, 2001; 15(3): 294 - 303.
[Abstract] [Full Text]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.