Identification of the Small Protein Rich in Arginine and Glycine (SRAG)

The characterization of new proteins will aid in our explanation of normal biology and disease. Toward that goal, we describe the initial characterization of the small protein rich in arginine and glycine (SRAG). Human and mouse SRAG are 248/249-amino acid arginine- and glycine-rich proteins that ar...

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Bibliographic Details
Published in:The Journal of biological chemistry 2009-05, Vol.284 (18), p.12504-12511
Main Authors: Zullo, Alfred J., Michaud, Monia, Zhang, Weiping, Grusby, Michael J.
Format: Article
Language:English
Subjects:
Molecular Basis of Cell and Developmental Biology
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Summary:The characterization of new proteins will aid in our explanation of normal biology and disease. Toward that goal, we describe the initial characterization of the small protein rich in arginine and glycine (SRAG). Human and mouse SRAG are 248/249-amino acid arginine- and glycine-rich proteins that are widely expressed in tissues and cell lines. Two SRAG isoforms, SRAG-5 and SRAG-3, which are truncations of full-length SRAG, were also identified. Although all SRAG proteins reside in the nucleus, they were also found within the nucleolus. Localization within the nucleolus was regulated by the N terminus of the protein. Our initial studies indicated that SRAG can interact with RNA. Full-length SRAG protein levels were highest in resting cells and were reduced in proliferating cells. The reduction in SRAG protein that occurs in proliferating cells was mapped with inhibitors to the G2/M phase of the cell cycle. As expected, the overexpression of SRAG reduced the percentage of cells in the G2/M phase and increased cell death. In sum, we have identified a new and intriguing member of the nucleolar proteome.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M809436200