JB Try AEM Online
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Groman, N. B.
Right arrow Articles by Suzuki, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Groman, N. B.
Right arrow Articles by Suzuki, G.
J Bacteriol. 1963 August; 86(2): 187-194
Copyright © 1963, The Williams & Wilkins Company. All Rights Reserved.

QUANTITATIVE STUDY OF ENDOLYSIN SYNTHESIS DURING REPRODUCTION OF LAMBDA PHAGES

Neal B. Groman and Grace Suzuki

Department of Microbiology, School of Medicine, University of Washington, Seattle, Washington

ABSTRACT

GROMAN, NEAL B. (University of Washington, Seattle) AND GRACE SUZUKI. Quantitative study of endolysin synthesis during reproduction of lambda phages. J. Bacteriol. 86:187–194. 1963.—Endolysin is presumed to be a phage-induced enzyme participating in lysis through its destructive action on the host cell wall. A method for assaying endolysin is described, which was utilized in studying endolysin synthesis at 37 and 44 C by induced strains of K-12 ({lambda}), K-12 ({lambda}tem), and K-12 ({lambda}112). In all cases, endolysin was detected prior to the appearance of mature, intracellular phage and was detected earlier at 44 C than at 37 C. It was synthesized at a linear rate, as was phage, and both syntheses terminated at the same time. Surprisingly, endolysin also accumulated under conditions in which induced K-12 ({lambda}112) exhibited lysis inhibition. Under these conditions, endolysin concentration per induced cell was 2 to 2.5 times that produced by normally lysing K-12 ({lambda}). Since alterations introduced into the lytic process by temperature, mutation, or both correlate well with the timing and rate of endolysin synthesis, the data tend to support the concept that endolysin determines the kinetics of the process. However, the accumulation of endolysin during lysis inhibition suggests the need for alternative hypotheses. One hypothesis is that although endolysin action is the key to lysis some preliminary steps are required to release the enzyme so that it may contact its substrate in the cell wall. A second hypothesis is that basically the lytic process involves an alteration in the permeability barrier of the cell and that lytic enzymes such as endolysin have evolved as an auxillary but dispensable mechanism to this process.


J Bacteriol. 1963 August; 86(2): 187-194
Copyright © 1963, The Williams & Wilkins Company. All Rights Reserved.







Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. Microbiol. Mol. Biol. Rev.
ALL ASM JOURNALS

Copyright © 1963 by the American Society for Microbiology. All rights reserved.