Skip Navigation

This Article
Right arrow Print PDF (426K)
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 Search for citing articles in:
ISI Web of Science (37)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Fang, G.-H.
Right arrow Articles by Hager, Lowell.P
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fang, G.-H.
Right arrow Articles by Hager, Lowell.P
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1986, Vol. 14, No. 20 8061-8071
© 1986

Articles

Cloning and sequencing of chloroperoxidase cDNA4

Guo-Hua Fang, Paul Kenigsberg1, Milton.J Axley2, Mark Nuell3 and Lowell.P Hager

Roger Adams Laboratory, Department of Biochemistry, University of Illinois Urbana, IL 61801, USA

Received September 2, 1986. Accepted September 22, 1986.

An oligod-d(T)12–18 primed cDNA library has been prepared from CaldaHo-myces fumago mRNA. A clone containing a full-length Insert was sequenced on the supercoiled plasmid, pBR322. The complete primary sequence of chloroper-oxidase has been derived. We have also determined about 73% of the peptide sequence by amino add sequencing. The DNA sequence data matches all of the available known peptide sequences. The mature polypeptide contains 300 amino adds having a combined molecular weight of 32, 974 daltons. A putative signal peptide of 21 amino adds is proposed from DNA sequence data. The chloroper-oxidase gene encodes three potential glycosylation sites recognized as Asn-X-Thr/Ser sequences. Three cysteine residues are found 1n the protein sequence. A small region around Cys87 bears a minimal homology to the active site of cytochrome P450cam. No other heme protein homologues can be detected. We propose that Cys87 serves as a thiolate ligand to the iron of heme prosthetic group. A rare arginine codon, AGG, is used three times out of twelve in contrast to the very infrequent use of this codon in E. coli or yeast.

1Present address: Department of Agronomy, USDA Physiology Laboratory, University of Illinois, Urbana, IL 61801

2Present address: Department of Biochemistry, National Institutes of Health-NHLBI, Room 102 Bldg.3, Bethesda, MD 20205

3Present address: Laboratory of Molecules Genetics, Gerontology research Center, 4940 Eastern Avenue, Baltimore, MD 21224, USA

*This work was supported by grants from the National Scheme Foundation, DMB 85-03599 and the National Institutes of Health, GM 07768


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
 Proc. Natl. Acad. Sci. USAHome page
X. Yi, M. Mroczko, K. M. Manoj, X. Wang, and L. P. Hager
Replacement of the proximal heme thiolate ligand in chloroperoxidase with a histidine residue
PNAS, October 26, 1999; 96(22): 12412 - 12417.
[Abstract] [Full Text] [PDF]

Home page
 ScienceHome page
J. Dawson
Probing structure-function relations in heme-containing oxygenases and peroxidases
Science, April 22, 1988; 240(4851): 433 - 439.
[Abstract] [PDF]


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.