Identification and Functional Analysis of SEDL-binding and Homologue Proteins by Immobilized GST Fusion and Motif Based Methods 


Vol. 29,  No. 2, pp. 381-388, Feb.  2008
10.5012/bkcs.2008.29.2.381


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  Abstract

An X-linked skeletal disorder, SEDT (spondyloepiphyseal dysplasia tarda) is a genetic disease characterized by a disproportionately short trunk and short stature caused by mutations in the SEDL gene. This gene is evolutionarily conserved from yeast to human. The yeast SEDL protein ortholog, Trs20p, has been isolated as a member of a large multi-protein complex called the transport protein particle (TRAPP), which is involved in endoplasmic reticulum (ER)-to-Golgi transport. The interaction between SEDL and partner proteins is important in order to understand the molecular mechanism of SEDL functions. We isolated several SEDLbinding proteins derived from rat cells by an immobilized GST-fusion method. Furthermore, the SEDLhomologue proteins were identified using motif based methods. Common motifs between SEDL-binding proteins and SEDL-homologue proteins were classified into seven types and 78 common motifs were revealed. Sequence similarities were contracted to seven types using phylogenetic trees. In general, types I-III and VI were classified as having the function of acetyl-CoA carboxylase, glycogen phosphorylase, isocitrate dehydrogenase, and enolase, respectively, and type IV was found to be functionally related to the GST protein. Types V and VII were found to contribute to TRAPP vesicle trafficking.

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  Cite this article

[IEEE Style]

J. Hong, M. S. Jeong, J. H. Kim, B. G. Kim, S. R. Holbrook, S. B. Jang, "Identification and Functional Analysis of SEDL-binding and Homologue Proteins by Immobilized GST Fusion and Motif Based Methods," Bulletin of the Korean Chemical Society, vol. 29, no. 2, pp. 381-388, 2008. DOI: 10.5012/bkcs.2008.29.2.381.

[ACM Style]

Ji-Man Hong, Mi Suk Jeong, Jae Ho Kim, Boo Gil Kim, Stephen R. Holbrook, and Se Bok Jang. 2008. Identification and Functional Analysis of SEDL-binding and Homologue Proteins by Immobilized GST Fusion and Motif Based Methods. Bulletin of the Korean Chemical Society, 29, 2, (2008), 381-388. DOI: 10.5012/bkcs.2008.29.2.381.

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ISSN(Print) 0253-2964
ISSN(Online) 1229-5949