Reference: Seog DH, et al. (1994) Molecular characterization of the USO1 gene product which is essential for vesicular transport in Saccharomyces cerevisiae. Biochem Biophys Res Commun 200(1):647-53

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Abstract


We have previously shown that USO1 gene required in the protein transport from the endoplasmic reticulum (ER) to the Golgi apparatus encodes a hydrophilic protein of 1790 amino acids. The sequence of carboxyl-terminal 1010 amino acids was predicted to have an alpha-helical structure characteristic of the coiled-coil rod region of the cytoskeleton-related proteins. Antibodies raised against partial sequences of the Uso1 polypeptide reacted with a 200 kDa protein in Western blots of the wild-type yeast proteins. The Uso1 protein was found predominantly in the soluble fraction and displayed a molecular mass of 800-900 kDa in gel filtration when globular protein were used as molecular mass standards. In sucrose density gradient centrifugation, however, the Uso1 protein cosedimented with a globular 6S marker protein, horseradish peroxidase (44 kDa). These results suggest that, in its native state, the Uso1 protein forms a nonglobular oligomer.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Seog DH, Kito M, Igarashi K, Yoda K, Yamasaki M
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