The N‐terminal prepeptide is required for the production of spore cortex‐lytic enzyme from its inactive precursor during germination of Clostridium perfringens S40 spores
The N‐terminal prepeptide is required for the production of spore cortex‐lytic enzyme from its inactive precursor during germination of Clostridium perfringens S40 spores
复制标题
在产气荚膜梭菌 S40 孢子萌发过程中,N 端前肽是从其无活性前体产生孢子皮质裂解酶所必需的
作者:
S. Okamura;K. Urakami;M. Kimata;T. Aoshima;S. Shimamoto;R. Moriyama;S. Makino
A spore cortex‐lytic enzyme of Clostridium perfringens S40 is synthesized during sporulation as a precursor consisting of four domains. After cleavage of an N‐terminal preregion and a C‐terminal proregion, inactive proenzyme (termed C35) is converted to active enzyme by processing of an N‐terminal prosequence with germination‐specific protease (GSP) during germination. The present results demonstrated that the cleaved N‐terminal prepeptide remained associated with C35. After the isolated complex was denatured and dissociated in 6 M urea solution, removal of urea regenerated a prepeptide–C35 complex which produces active enzyme when incubated with GSP. However, isolated C35 alone could not be activated by GSP. The prepeptide–C35 complex was more heat stable than active enzyme. Thus, non‐covalent attachment of the prepeptide to C35 is required to assist correct folding of C35 and to stabilize its conformation, suggesting that the prepeptide functions as an intramolecular chaperone. Recombinant proteins, which have prepeptide covalently bonded to C35, were processed by GSP as well as the in vivo prepeptide–C35 complex, and the full length of the N‐terminal presequence was needed to fulfil its role. Although the C‐terminal prosequence is present as an independent domain which is not involved in the activation process of the enzyme, it appears that the N‐terminal prosequence contributes to the regulation of enzyme activity as an inhibitor of the enzyme.
DOI:
10.1016/s0021-9258(18)61070-1
发表时间:
1987-07
期刊:
The Journal of biological chemistry
影响因子:
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作者:
P. Matsudaira
通讯作者:
P. Matsudaira