Archaeal Aminoacyl-tRNA Synthesis: Diversity Replaces Dogma

Authors

Debra Tumbula, Yale University
Ute C. Vothknecht, Yale University
Hyun-soo Kim, Yale University
Michael Ibba, Chapman UniversityFollow
Bokkee Min, Yale University
Tong Li, Yale University
Joanne Pelaschier, Yale University
Constantinos Stathopoulos, Yale University
Hubert D. Becker, Yale University
Dieter Söll, Yale University

Document Type

Article

Publication Date

8-1-1999

Abstract

The essential protein lysyl-tRNA synthetase (LysRS) exists in two unrelated forms, a class I and a class II-type aminoacyl-tRNA synthetase. Comparative genome sequence analysis revealed that Borrelia burgdorferi sensu lato, the etiological agent of Lyme disease, contains a class I-type LysRS, whereas its tick and mammalian hosts would be expected to contain a class II-type protein. To investigate the utility of the class I LysRS as a diagnostic target for Lyme disease, the corresponding gene (lysK) was cloned and sequenced from B. afzelii, B. garinii, and B. hermsii. These lysK sequences were then used to design a primer set that could detect and genotype B. burgdorferi sensu strictu, B. afzelii, and B. garinii in one single polymerase chain reaction, while showing no cross reactivity with examples of other Borrelia or spirochetes.

Comments

This article was originally published in Genetics, volume152, in 1999.

Recommended Citation

Tumbula, D., Vothknecht, U.C., Kim, H-S., Ibba, M., Min, B., Li, T., Pelaschier, J., Stathopoulos, C., Becker, H. and Söll, D. (1999) Archaeal aminoacyl-tRNA synthesis: diversity replaces dogma. Genetics 152, 1269-1276.

Copyright

Genetics Society of America