Sequence and characterization of an Ehrlichia chaffeensis gene encoding 314 amino acids highly homologous to the NAD A enzyme.

Abstract:

:DNA sequence analysis of the nadA gene of Ehrlichia chaffeensis revealed a 942 bp open reading frame with the capacity to encode 314 amino acids. The amino acid sequence of the E. chaffeensis quinolinate synthetase A (NAD/A) has 53.6% identity and 82% similarity to the NAD A of the cyanelle of Cyanophora paradoxa. Portions of the homologous genes of E. canis and E. muris were also sequenced. The amino acid sequences of the NAD A of E. canis and E. muris have 89.2% and 93.2% homology, respectively, to the NAD A of E. chaffeensis. We propose that the nadA gene may be an excellent candidate for a genetic tool for the phylogenetic study of ehrlichiae.

journal_name

FEMS Microbiol Lett

authors

Yu XJ,Walker DH

doi

10.1111/j.1574-6968.1997.tb12623.x

subject

Has Abstract

pub_date

1997-09-01 00:00:00

pages

53-8

issue

1

eissn

0378-1097

issn

1574-6968

pii

S0378-1097(97)00300-5

journal_volume

154

pub_type

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