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J Bacteriol. 1965 Sep;90(3):575-88.

Replacement of Lysine by Hydroxylysine and Its Effects on Cell Lysis in Streptococcus faecalis.

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  • 1Department of Microbiology, Temple University School of Medicine, Philadelphia, Pennsylvania.

Abstract

Shockman, Gerald D. (Temple University, Philadelphia, Pa.), J. Stuart Thompson, and Margaret J. Conover. Replacement of lysine by hydroxylysine and its effects on cell lysis in Streptococcus faecalis. J. Bacteriol. 90:575-588. 1965.-Hydroxylysine was not significantly incorporated by Streptococcus faecalis ATCC 9790 or 8043 until exponential growth ceased as a result of lysine exhaustion. Uptake was then rapid and virtually complete within 1 hr. Lysine absence, rather than physiological age, seemed to be the governing factor. Hydroxylysine uptake rapidly reached a peak in the acid-soluble fraction, suggesting a precursor role for substances in this fraction. Substitution of hydroxylysine for lysine was much more efficient in mucopeptide synthesis than in protein synthesis. In wall medium, less than 1% of the incorporated hydroxylysine was found in the protein fraction. Addition of lysine to both growth and wall media inhibited both further hydroxylysine uptake and transfer of hydroxylysine from acid-soluble to mucopeptide or protein fractions. Hydroxylysine resulted in decreased penicillin susceptibility only after it was postexponentially incorporated. This effect was physiologically similar to that seen after threonine deprivation or chloramphenicol treatment. Hydroxylysine incorporation increased resistance to autolysis, but failed to decrease lysozyme susceptibility when measured after heat inactivation of autolysis. Electron microscopy of negatively stained cells showed increased thickness of cell walls containing hydroxylysine. Thus, most of the effects of replacement of lysine by hydroxylysine resemble those seen after deprivation of a nonwall amino acid (e.g., threonine or valine) or after chloramphenicol treatment. Each of these conditions results in inhibition of protein synthesis while permitting cell-wall synthesis to continue, resulting in autolysis-resistant, thick-walled cells.

PMID:
16562051
[PubMed]
PMCID:
PMC315694
Free PMC Article
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