Purification and polar localization of pneumococcal LytB, a putative endo-beta-N-acetylglucosaminidase: the chain-dispersing murein hydrolase.

@article{Rivas2002PurificationAP,
  title={Purification and polar localization of pneumococcal LytB, a putative endo-beta-N-acetylglucosaminidase: the chain-dispersing murein hydrolase.},
  author={Blanca de las Rivas and J{\'e}ssica Leite Garcia and R. Vara Lopez and Pedro Garc{\'i}a},
  journal={Journal of bacteriology},
  year={2002},
  volume={184 18},
  pages={4988-5000}
}
The DNA region encoding the mature form of a pneumococcal murein hydrolase (LytB) was cloned and expressed in Escherichia coli. LytB was purified by affinity chromatography, and its activity was suggested to be the first identified endo-beta-N-acetylglucosaminidase of Streptococcus pneumoniae. LytB can remove a maximum of only 25% of the radioactivity from [(3)H]choline-labeled pneumococcal cell walls in in vitro assays. Inactivation of the lytB gene of wild-type strain R6 (R6B mutant) led to… CONTINUE READING

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In contrast , translational fusion protein GFP - LytA preferentially bound to the equatorial regions of choline - containing cells but did not affect their average chain length .
The GFP - LytB fusion protein was also able to unchain the lytB mutants but not the EA cells .
In contrast , translational fusion protein GFP - LytA preferentially bound to the equatorial regions of choline - containing cells but did not affect their average chain length .
The GFP - LytB fusion protein was also able to unchain the lytB mutants but not the EA cells .
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