Abstract
Previously, two genes, designated as lyt and hol, were identified in the lysis module of phage μ1/6. They were cloned and expressed in Escherichia coli. An additional candidate holin gene, hol2, was found downstream from the hol gene based on one predicted transmembrane domain and a highly charged C-terminal sequence of the encoded protein. Expression of hol or hol2 in E. coli was shown to cause cell death. The concomitant expression of λ endolysin (R) and μ1/6 holin resulted in cell lysis. Similarly, the coexpression of the endolysin and holin of phage μ1/6 led to lysis, apparently due to the ability of μ1/6 endolysin to hydrolyze the peptidoglycan layer of this bacterium. In contrast, the simultaneous expression of μ1/6 hol2 and the endolysin gene (λR or μ1/6 lyt) did not cause detectable lysis of the host cells. Demonstration of the holin function in streptomycetes was achieved by providing for the release of μ1/6 endolysin to the periplasm and subsequent cleavage of the peptidoglycan, which strongly suggested that the holin produces lesions in the streptomycete membrane.
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This work was supported by VEGA grant no. 2/0121/25 of the Slovak Academy of Sciences.
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Farkašovská, J., Godány, A. The Lysis System of the Streptomyces aureofaciens Phage μ1/6. Curr Microbiol 57, 631–637 (2008). https://doi.org/10.1007/s00284-008-9255-0
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DOI: https://doi.org/10.1007/s00284-008-9255-0