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J. Biol. Chem., Vol. 282, Issue 28, 20200-20206, July 13, 2007

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Regulation of Mammalian Protein O-Mannosylation

PREFERENTIAL AMINO ACID SEQUENCE FOR O-MANNOSE MODIFICATION^*

Hiroshi Manya, Takehiro Suzuki^¶, Keiko Akasaka-Manya, Hide-Ki Ishida^||, Mamoru Mizuno^**, Yasushi Suzuki, Toshiyuki Inazu, Naoshi Dohmae^¶, and Tamao Endo¹

From the Glycobiology Research Group, Tokyo Metropolitan Institute of Gerontology, Foundation for Research on Aging and Promotion of Human Welfare, Itabashi-ku, Tokyo 173-0015, Biomolecular Characterization Team, RIKEN, Wako-shi, Saitama 351-0198, ^¶Japan Science and Technology Agency CREST, ^||Tokyo Chemical Industry Co., Ltd., Kita-ku, Tokyo 114-0003, ^**Research Department, The Noguchi Institute, Itabashi-ku, Tokyo 173-0003, and Department of Applied Chemistry, School of Engineering and Institute of Glycotechnology, Tokai University, Hiratsuka-shi, Kanagawa 259-1292, Japan

O-Mannosyl glycans are important in muscle and brain development. Protein O-mannosyltransferase (POMT) catalyzes the initial step of O-mannosyl glycan biosynthesis. To understand which serine (Ser) and threonine (Thr) residues POMT recognizes for mannosylation, we prepared a series of synthetic peptides based on a mucin-like domain in -dystroglycan (-DG), one of the best known O-mannosylated proteins in mammals. In -DG, the mucin-like domain spans amino acid residues 316 to 489. Two similar peptide sequences, corresponding to residues 401–420 and 336–355, respectively, were strongly mannosylated by POMT, whereas other peptides from -DG and peptides of various mucin tandem repeat regions were poorly mannosylated. Peptides 401–420 and 336–355 contained four and six Ser and Thr residues, respectively. Substitution of Ala residues for the Ser or Thr residues showed that Thr-414 of peptide 401–420 and Thr-351 of peptide 336–355 were prominently modified by O-mannosylation. Matrix-assisted laser desorption ionization time-of-flight mass spectrometry and Edman degradation analysis of the mannosylated peptide 401–420 indicated that Thr-414 was the Thr residue that was most prominently modified by O-mannosylation and that O-mannosylation occurred sequentially rather than at random. Based on these results, we propose a preferred amino acid sequence for mammalian O-mannose modification.

Received for publication, March 20, 2007 , and in revised form, April 20, 2007.

^* This study was supported by a research grant for nervous and mental disorders (17A-10) and research on psychiatric and neurological diseases and mental health from the Ministry of Health, Labor, and Welfare of Japan, a grant-in-aid for scientific research on priority area (14082209) and on scientific research (17657039) from the Ministry of Education, Culture, Sports, Science, and Technology of Japan, and the Japan Society for the Promotion of Science Core-to-Core Program. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1–S5.

¹ To whom correspondence should be addressed: Glycobiology Research Group, Tokyo Metropolitan Institute of Gerontology, Foundation for Research on Aging and Promotion of Human Welfare, 35-2 Sakaecho, Itabashi-ku, Tokyo 173-0015, Japan. Tel.: 81-3-3964-3241 (ext. 3080); Fax: 81-3-3579-4776; E-mail: endo{at}tmig.or.jp.

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