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J. Bacteriol., 10 1995, 5460-5466, Vol 177, No. 19
LA Fernandez-Herrero, G Olabarria, JR Caston, I Lasa and J Berenguer
The S-layers of Thermus thermophilus HB27 and T. thermophilus HB8 are
composed of protein units of 95 kDa (P95) and 100 kDa (P100), respectively.
We have selected S-layer deletion mutants from both strains by complete
replacement of the slpA gene. Mutants of the two strains showed similar
defects in growth and morphology and overproduced an external cell envelope
inside of which cells remained after division. However, the nature of this
external layer is strain specific, being easily stained and regular in the
HB8 delta slpA derivative and amorphous and poorly stained in the HB27
delta slpA strain. The addition of chromosomic DNA from T. thermophilus HB8
to growing cultures of T. thermophilus HB27 delta slpA led to the selection
of a new strain, HB27C8, which expressed a functional S-layer composed of
the P100 protein. Conversely, the addition of chromosomic DNA from T.
thermophilus HB27 to growing cultures of T. thermophilus HB8 delta slpA
allowed the isolation of strain HB8C27, which expressed a functional
S-layer composed of the P95 protein. The driving force which selected the
transference of the S-layer genes in these experiments was the difference
in growth rates, one of the main factors leading to selection in natural
environments.
Copyright © 1995, American Society for Microbiology
Horizontal transference of S-layer genes within Thermus thermophilus
Centro de Biologia Molecular Severo Ochoa, Universidad Autonoma de Madrid-Consejo, Spain.
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