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The Zymogen of the Protease That Degrades Small, Acid-soluble Proteins of Spores of Bacillus Species Can Rapidly Autoprocess to the Active Enzyme in Vitro

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Journal J Bacteriol
Specialty Microbiology
Date 1994 Sep 1
PMID 8071242
Citations 5
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Abstract

The zymogen of the protease (GPR) that initiates protein degradation during spore germination in Bacillus species is not activated in vitro under normal physiological conditions. However, there is rapid, acid-pH-dependent, zero-order, proteolytic activation of the purified zymogen in high concentrations of dimethyl sulfoxide. These findings provide further evidence that GPR activates itself during sporulation.

Citing Articles

Site-directed mutagenesis and structural studies suggest that the germination protease, GPR, in spores of Bacillus species is an atypical aspartic acid protease.

Carroll T, Setlow P J Bacteriol. 2005; 187(20):7119-25.

PMID: 16199582 PMC: 1251623. DOI: 10.1128/JB.187.20.7119-7125.2005.


Structure and mechanism of action of the protease that degrades small, acid-soluble spore proteins during germination of spores of Bacillus species.

Nessi C, Jedrzejas M, Setlow P J Bacteriol. 1998; 180(19):5077-84.

PMID: 9748439 PMC: 107542. DOI: 10.1128/JB.180.19.5077-5084.1998.


Most of the propeptide is dispensable for stability and autoprocessing of the zymogen of the germination protease of spores of Bacillus species.

Pedersen L, Nessi C, Setlow P J Bacteriol. 1997; 179(5):1824-7.

PMID: 9045848 PMC: 178901. DOI: 10.1128/jb.179.5.1824-1827.1997.


Properties of Bacillus subtilis small, acid-soluble spore proteins with changes in the sequence recognized by their specific protease.

Setlow P J Bacteriol. 1994; 176(17):5357-63.

PMID: 8071212 PMC: 196721. DOI: 10.1128/jb.176.17.5357-5363.1994.


Autoprocessing of the protease that degrades small, acid-soluble proteins of spores of Bacillus species is triggered by low pH, dehydration, and dipicolinic acid.

Illades-Aguiar B, Setlow P J Bacteriol. 1994; 176(22):7032-7.

PMID: 7961468 PMC: 197077. DOI: 10.1128/jb.176.22.7032-7037.1994.

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