Purification and characterization of a 60-kDa protein from oat, formerly known as a TCP1-related chaperone |
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Authors: | William Parker Todd A. Wells Susanne Meza-Keuthen In-Soo Kim Pill-Soon Song |
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Affiliation: | (1) Department of Chemistry, University of Nebraska, 68588-0304 Lincoln, Nebraska;(2) Department of Genetic Engineering, Kyungpuk National University, Taegu, Korea |
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Abstract: | Recently, Mummertet al. [Nature363, 644–648 (1993)] isolated a proposed TCP1-related chaperone. Here we report several findings concerning the protein which they sequenced. Two similar N-terminal sequences were obtained from this abundant 60-kDa protein. Internal sequences were also acquired by protease digestion. Initially it was believed the protein was able to completely inhibit citrate synthase aggregation, but later purifications demonstrated that the 60-kDa polypeptide lacked both chaperone activity and the previously reported kinase activity [Grimmet al., Planta178, 199–206 (1989)]. It is now our belief that this protein is neither a chaperone nor a kinase. |
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Keywords: | Chaperone TCP1 Avena sativa glucosidase |
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