JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


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
Right arrow Citation Map
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 Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Fonzi, W. A.
Right arrow Articles by Sypherd, P. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fonzi, W. A.
Right arrow Articles by Sypherd, P. S.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J. Biol. Chem., Vol. 262, Issue 21, 10127-10133, 07, 1987

The gene and the primary structure of ornithine decarboxylase from Saccharomyces cerevisiae

WA Fonzi and PS Sypherd

The nucleotide sequence was determined for a 3-kilobase genomic fragment containing the ornithine decarboxylase gene of Saccharomyces cerevisiae. The fragment contained two open reading frames. Gene disruption localized the ornithine decarboxylase gene to a 1398- nucleotide open reading frame. Transcription of the yeast gene initiated at several sites 171 to 211 nucleotides 5' of the translational start site. The 3' end of the transcript extended approximately 300 nucleotides beyond the end of the ornithine decarboxylase coding region and contained two copies of the yeast ARS core sequence. Translation of the ornithine decarboxylase gene appeared to initiate at the first AUG condon of the open reading frame based upon translational fusions with the Escherichia coli beta-galactosidase gene. Since no introns were apparent, the 1398-nucleotide open reading frame was predicted to encode a 466-amino acid protein with a calculated Mr = 52,369. The deduced protein differed significantly in size from previous reports on yeast ornithine decarboxylase, but was very similar in size to mammalian ornithine decarboxylase. When the predicted amino acid sequence of yeast ornithine decarboxylase was compared with that of the mouse enzyme, alignment of the sequences revealed that 40% of the amino acid residues were identical. Chou- Fasman predictions of the secondary structure of the two enzymes indicated that secondary structure was also highly conserved.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
M. A. Hoyt, M. Zhang, and P. Coffino
Ubiquitin-independent Mechanisms of Mouse Ornithine Decarboxylase Degradation Are Conserved between Mammalian and Fungal Cells
J. Biol. Chem., March 28, 2003; 278(14): 12135 - 12143.
[Abstract] [Full Text] [PDF]


Home page
MicrobiologyHome page
Y. Nakada and Y. Itoh
Identification of the putrescine biosynthetic genes in Pseudomonas aeruginosa and characterization of agmatine deiminase and N-carbamoylputrescine amidohydrolase of the arginine decarboxylase pathway
Microbiology, March 1, 2003; 149(3): 707 - 714.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
A. Bailey, E. Mueller, and P. Bowyer
Ornithine Decarboxylase of Stagonospora (Septoria) nodorum Is Required for Virulence toward Wheat
J. Biol. Chem., May 5, 2000; 275(19): 14242 - 14247.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
C. Toth and P. Coffino
Regulated Degradation of Yeast Ornithine Decarboxylase
J. Biol. Chem., September 3, 1999; 274(36): 25921 - 25926.
[Abstract] [Full Text] [PDF]


Home page
Infect. Immun.Home page
A. B. Herrero, M. C. Lopez, S. Garcia, A. Schmidt, F. Spaltmann, J. Ruiz-Herrera, and A. Dominguez
Control of Filament Formation in Candida albicans by Polyamine Levels
Infect. Immun., September 1, 1999; 67(9): 4870 - 4878.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
D. Alabadí and J. Carbonell
Expression of Ornithine Decarboxylase Is Transiently Increased by Pollination, 2,4-Dichlorophenoxyacetic Acid, and Gibberellic Acid in Tomato Ovaries
Plant Physiology, September 1, 1998; 118(1): 323 - 328.
[Abstract] [Full Text]


Home page
Proc. Natl. Acad. Sci. USAHome page
F. Svensson, C. Ceriani, E. L. Wallstrom, I. Kockum, I. D. Algranati, O. Heby, and L. Persson
Cloning of a trypanosomatid gene coding for an ornithine decarboxylase that is metabolically unstable even though it lacks the C-terminal degradation domain
PNAS, January 21, 1997; 94(2): 397 - 402.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
Y. Murakami, T. Ichiba, S. Matsufuji, and S.-i. Hayashi
Cloning of Antizyme Inhibitor, a Highly Homologous Protein to Ornithine Decarboxylase
J. Biol. Chem., February 16, 1996; 271(7): 3340 - 3342.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1987 by the American Society for Biochemistry and Molecular Biology.