Skip Navigation

This Article
Right arrow Print PDF (2635K)
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 (66)
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Aimi, J.
Right arrow Articles by Dixon, J. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Aimi, J.
Right arrow Articles by Dixon, J. E.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1990, Vol. 18, No. 22 6665-6672
© 1990

MOLECULAR BIOLOGY

De novo purine nucleotide biosynthesis: cloning of human and avian cDNAs encoding the trifunctional glycinamide ribonucleotide synthetase-aminoimidazole ribonucleotide synthetase-glycinamide ribonucleotide transformylase by functional complementation in E.coli

Junko Aimi, Hong Qiu, John Williams, Howard Zalkin and Jack E. Dixon*

Purdue University, Department of Biochemistry West Lafayette, IN 47907, USA

* To whom correspondence should be addressed

Received May 18, 1990. Revised August 8, 1990. Accepted August 8, 1990.

The trifunctional enzyme encoding glycinamide ribonucleotide synthetase (GARS)-aminolmidazole ribonucleotide synthetase(AIRS)-glycinamide ribonucleotide transformylase (GART) was cloned by functional complementation of an E. coli mutant using an avlan liver cDNA expression library. In E. coli, genes encoding these separate activities (purD, purM, and purN, respectively) produce three proteins. The avian cDNA, in contrast, encodes a single polypeptide with all three enzyme activities. Using the avian DNA as a probe, a cDNA encoding the complete coding sequence of the trifunctional human enzyme was also isolated and sequenced. The deduced amino acid sequence of the human and avian polyproteins show extensive sequence homologies to the bacterial purD, purM, and purN encoded proteins. Avian and human liver RNAs appear to encode both a trifunctional enzyme (G-ARS-AIRS-GART) as well as an RNA which encodes only GARS. The trifunctional protein has been implicated in the pathology of Downs Syndrome and molecular tools are now available to explore this hypothesis. Initial efforts to compare the expression of GARS-AIRS-GART between a normal fibroblast cell line and a Downs Syndrome cell line indicate that the levels of RNA are similar.


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
 J. Biol. Chem.Home page
V. D. Antle, D. Liu, B. R. McKellar, C. A. Caperelli, M. Hua, and R. Vince
Substrate Specificity of Glycinamide Ribonucleotide Synthetase from Chicken Liver
J. Biol. Chem., April 5, 1996; 271(14): 8192 - 8195.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. L. C. Kan and R. G. Moran
Analysis of a Mouse Gene Encoding Three Steps of Purine Synthesis Reveals Use of an Intronic Polyadenylation Signal without Alternative Exon Usage
J. Biol. Chem., January 27, 1995; 270(4): 1823 - 1832.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
L. T. Gooljarsingh, J. Ramcharan, S. Gilroy, and S. J. Benkovic
Localization of GAR transformylase in Escherichia coli and mammalian cells
PNAS, June 5, 2001; 98(12): 6565 - 6570.
[Abstract] [Full Text] [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.