Open AccessSequence and characterization of an Ehrlichia chaffeensis gene encoding 314 amino acids highly homologous to the NAD A enzyme
Author(s) -
Yu Xuejie,
Walker David H.
Publication year - 1997
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1997.tb12623.x
Subject(s) - ehrlichia chaffeensis , biology , nad+ kinase , gene , homology (biology) , peptide sequence , amino acid , nucleic acid sequence , genetics , sequence analysis , microbiology and biotechnology , open reading frame , biochemistry , polymerase chain reaction , enzyme
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.