Deletion analysis of the proteinase gene of Streptococcus cremoris Wg2.
The Streptococcus cremoris Wg2 proteinase gene, cloned in S. lactis, specified a proteinase which exhibited the same specificity toward casein as did the proteinase isolated from the original host. Although the cloned gene lacked the last 130 codons, the proteinase still specifically degraded beta-casein. Deletion of the C-terminal 343 amino acids from the proteinase did not influence this specificity. Cell-free transcription-translation studies of plasmids carrying deletion derivatives of the proteinase gene showed that the 100-kilodalton C-terminally truncated proteinase still exhibited proteolytic activity. Crossed immunoelectrophoresis revealed that proteins A and B identified in the proteolytic system of S. cremoris Wg2 are both encoded by the proteinase gene. A working model based on integration of available genetic, immunological, and biochemical data is presented to explain this result.
Kok
J
J
Institute of Genetics, University of Groningen, Haren, The Netherlands.
Hill
D
D
Haandrikman
A J
AJ
de Reuver
M J
MJ
Laan
H
H
Venema
G
G
D000595:Amino Acid Sequence; D002872:Chromosome Deletion; D003378:Counterimmunoelectrophoresis; D010450:Endopeptidases / Q000032:analysis / Q000235:genetics*; D008970:Molecular Weight; D014176:Protein Biosynthesis; D013291:Streptococcus / Q000201:enzymology* / Q000235:genetics; D014158:Transcription, Genetic
D010450:Endopeptidases