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Isoschizomers of the restriction endonuclease Taql (T/CGA) requiring different metal ion concentrations and having a range of thermal stabilities from Thermus species from different continents

Article Abstract:

A study is conducted to determine the existence of thermophilic Type II restriction endonuclease Taql in 152 isolates of the genus Thermus derived from hot springs located in four continents. 27 isolates were observed to contain isoschizomers of Taql. Six of these isolates were identified as Thermus species T. brockianus, T. scotoductus, T. thermophilus, T. filiformis and T. aquaticus. They vary with regard to thermal stability, isoelectric points, magnesium ion needs and subunit molecular masses.

Author: Welch, Simon G., Al-Awadhi, Sameera, Williams, Ralph A.D.
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1998
Genetic aspects, Bacteria, Thermophilic, Restriction enzymes, DNA, DNA restriction enzymes, Thermophiles

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Mitogenic factor secreted by Streptococcus pyogenes is a heat-stable nuclease requiring His122 for activity

Article Abstract:

The mitogenic factor (MF) of Streptococcus pyogenes was analyzed. MF was cloned from S. pyogenes and its recombinant was overexpressed in Escherichia coli. It was found that both natural and recombinant MF exhibit heat-resistant nuclease activity. Results suggest that MF may play a role in pathogenesis as those with other pyrogenic exotoxins and may have various role in the pathogenesis of group A streptococcal infection.

Author: Iwasaki, Makoto, Igarashi, Hisanaga, Yutsudo, Takashi
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1997
Streptococcus pyogenes, Nucleases

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SepA, the 110 kDa protein secreted by Shingella flexneri: two-domain structure and proteolytic activity

Article Abstract:

The potential proteolytic activity and two-domain structure of sepA was determined in an experiment. This 110 kDa protein secreted by the Shigella flexneri was suspected to play a role in the invasion and destruction of the intestinal epithelium. Results showed that sepA did not affect the the aggregation of human platelets. Moreover, the protein was characterized by two domains with varying residues.

Author: Montecucco, Cesare, Sansonetti, Philippe J., Benjelloun-Touimi, Zineb, Si Tahar, Mustapha, Parsot, Claude
Publisher: Society for General Microbiology
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1998
Bacterial proteins, Shigella flexneri

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