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

Xue Jie Yu, David Walker

Research output: Contribution to journalArticle

17 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)53-58
Number of pages6
JournalFEMS Microbiology Letters
Volume154
Issue number1
DOIs
StatePublished - Sep 1 1997

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Ehrlichia chaffeensis
NAD
Amino Acids
Enzymes
Genes
Cyanophora
Amino Acid Sequence
Ehrlichia
DNA Sequence Analysis
Open Reading Frames

Keywords

  • Cyanelle
  • Ehrlichia chaffeensis
  • nadA gene

ASJC Scopus subject areas

  • Genetics
  • Molecular Biology
  • Applied Microbiology and Biotechnology
  • Microbiology

Cite this

Sequence and characterization of an Ehrlichia chaffeensis gene encoding 314 amino acids highly homologous to the NAD A enzyme. / Yu, Xue Jie; Walker, David.

In: FEMS Microbiology Letters, Vol. 154, No. 1, 01.09.1997, p. 53-58.

Research output: Contribution to journalArticle

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