Cloning and isolation of a Conus cysteine-rich protein homologous to Tex31 but without proteolytic activity.

Acta Biochim Biophys Sin (Shanghai)

Institute of Protein Research, Tongji University, Shanghai 200092, China.

Published: February 2008

We cloned and isolated a cysteine-rich protein, designated Mr30, from Conus marmoreus. Mr30 belongs to the cysteine-rich secretory protein family that is highly homologous to Tex31 previously obtained from Conus textile and reported as a protease responsible for processing of pro-conotoxins. Mr30, purified by a procedure similar to that of Tex31, indeed showed low proteolytic activity. However, further investigations revealed that the detected protease activity actually resulted from a trace amount of protease(s) contamination rather than from Mr30 itself. This finding led us to rethink the role of conus cysteine-rich secretory proteins: they were probably not responsible for the processing of pro-conotoxins as previously deduced, but their real biological functions remained to be clarified.

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Source
http://dx.doi.org/10.1111/j.1745-7270.2008.00385.xDOI Listing

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