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A prokaryotic-type cytidine deaminase from Arabidopsis thaliana gene expression and functional characterization.

Authors :
Faivre-Nitschke SE
Grienenberger JM
Gualberto JM
Source :
European journal of biochemistry [Eur J Biochem] 1999 Aug; Vol. 263 (3), pp. 896-903.
Publication Year :
1999

Abstract

The gene and cDNA of an Arabidopsis thaliana cytidine deaminase (CDA) were cloned and sequenced. The gene, At-cda1, is located on chromosome 2 and is expressed in all plant tissues tested, although with quantitative differences. Expression analysis suggest that At-cda1 probably codes for the housekeeping cytidine deaminase of Arabidopsis. The gene was functionally expressed in Escherichia coli and the protein, At-CDA1, shows similar enzymatic and substrate specificities as conventional cytidine deaminases: it deaminates cytidine and deoxycytidine and is competitively inhibited by cytosine-containing compounds. Because the protein shows no affinity to RNA, it is not likely to be involved in RNA-editing by C-to-U deamination. When compared to cytidine deaminases from other organisms, it becomes clear that At-CDA1 is related, both in sequence and structure, to the CDA of E. coli and other gram-negative bacteria. The eubacterial nature of the Arabidopsis CDA suggests that it is an additional example of a plant gene of endosymbiotic origin.

Details

Language :
English
ISSN :
0014-2956
Volume :
263
Issue :
3
Database :
MEDLINE
Journal :
European journal of biochemistry
Publication Type :
Academic Journal
Accession number :
10469156
Full Text :
https://doi.org/10.1046/j.1432-1327.1999.00591.x