Research Article
Dictyostelium Genes Dysregulated in an O-Glycosylation Mutant Identified by mRNA Differential Display
Motonobu Yoshida1*, Naoya Sakuragi1, Eiji Tanesaka1 and Yutaka Sendai21Department of Agricultural Science, Kinki University, Nakamachi, Nara 631-8505, Japan
2Research Institute for the Functional Peptides, Shimojyo-cho, Yamagata 990-0823, Japan
- Corresponding Author:
- Motonobu Yoshida
Department of Agricultural Science, Kinki University
Nakamachi, Nara 631-8505, Japan
Tel: +81 742 43 5245
Fax: +81 742 43 1155
E-mail: yoshida_m@nara.kindai.ac.jp
Received date: October 27, 2012; Accepted date: November 29, 2012; Published date: December 02, 2012
Citation: Yoshida M, Sakuragi N, Tanesaka E, Sendai Y (2012) Dictyostelium Genes Dysregulated in an O-Glycosylation Mutant Identified by mRNA Differential Display. J Biotechnol Biomater 2:152. doi:10.4172/2155-952X.1000152
Copyright: © 2012 Yoshida M, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Abstract
Seven differentially-expressed cDNA clones were isolated by using an mRNA differential display between a Dictyostelium wild-type AX2 and a mutant HG794 defective in O-glycosylation. Transcript levels for the seven clones were reduced or not detectable in the mutant HG794. Homology search showed that the four cDNA clones, DD-3 and DD-7~9 are novel and that three cDNA clones, DD-4 and DD-5, -6 encode an actin-bundling protein and phosphodiesterase inhibitors, respectively. Full-length cDNAs for DD-3 and -8 were isolated and labeled DD3-3 and DD8-14, respectively. DD3-3 consists of 2,166 bp and DD8-14 of 2,084 bp. DD3-3 was preliminarily reported in a previous paper [1]. SSL850 was named a clone by the “Dictyostelium cDNA Project in Japan”, containing a fulllength cDNA for DD-7 and was labeled DD7-1 of 902 bp. It has 60% homology with discoidin Ia. DD8-14 most likely has no direct role in glycosylation, while DD3-3 and DD7-1 very likely are involved in some aspect of recognition of glycosylation.