This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Friede, J. D. Articles by Henderson, L. M. Search for Related Content PubMed PubMed Citation Articles by Friede, J. D. Articles by Henderson, L. M.

 Previous Article  |  Next Article 

J Bacteriol. 1972 January; 109(1): 179-185
Copyright © 1972 American Society for Microbiology. All Rights Reserved.

Transport of Lysine and Hydroxylysine in Streptococcus faecalis¹

^a Department of Biochemistry, College of Biological Sciences, University of Minnesota, St. Paul, Minnesota 55101

ABSTRACT

Data are presented which support the view that L-lysine is transported by two systems in Streptococcus faecalis. The system with the higher affinity for L-lysine appears to be specific for L-lysine among the common amino acids and to require an energy source. The second system transports both L-lysine and L-arginine and does not appear to require an energy source. Both of these systems will accept hydroxy-L-lysine as a substrate as shown by the energy requirement for hydroxy-L-lysine transport and by the inhibition of uptake by L-arginine as well as by L-lysine. The affinity of both systems appears to be considerably lower for hydroxy-L-lysine than for L-lysine. A mutant of S. faecalis which is resistant to the growth inhibitory action of hydroxy-L-lysine appears to differ from the parent strain by having a defective L-lysine-specific transport system. In this mutant, hydroxy-L-lysine is not readily transported via the L-lysine-specific system because of the mutation or via the second system because of the high concentration of L-arginine present in the growth medium. This overall lack of transport prevents hydroxy-L-lysine from reaching inhibitory levels within the cell.

² Present address: Department of Biochemistry, Oklahoma State University, Stillwater, Okla. 74074.

³ Present address: Veterans Hospital, Minneapolis, Minn. 55455.

¹ Part of a thesis submitted by J. D. Friede to the Graduate School of the University of Minnesota, 1970, in partial fulfillment of the requirements for the Ph.D. degree.