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

Journal of Bacteriology

Volumn 179, Issue 5, 1997, Pages 1824-1827

  Pedersen, Lotte Bang ^a   Nessi, Claudio ^b   Setlow, Peter ^b  

^a AARHUS UNIVERSITY   (Denmark)

^b UNIVERSITY OF CONNECTICUT HEALTH CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; ENZYME PRECURSOR; PROTEINASE;

AMINO TERMINAL SEQUENCE; ARTICLE; BACILLUS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; GERMINATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; SPOROGENESIS;

BACTERIA (MICROORGANISMS);

EID: 0031058134     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.5.1824-1827.1997     Document Type: Article

References (14)

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4. Illades-Aguiar, B., and P. Setlow. 1994. 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. J. Bacteriol. 176:5571-5573.
5. Illades-Aguiar, B., and P. Setlow. 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. J. Bacteriol. 176:7032-7037.
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9. Nessi, C., and P. Setlow. 1996. Unpublished results.
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13. Setlow, P. 1993. Spore structural proteins, p. 801-809. In J. A. Hoch, R. Losick, and A. L. Sonenshein (ed.), Bacillus subtilis and other gram-positive bacteria: biochemistry, physiology, and molecular genetics. American Society for Microbiology, Washington, D.C.
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