Dictyostelium gnt15 encodes a protein with similarity to LARGE and plays an essential role in development

Pang, Te Ling; Wu, Chao-Jung; Chen, Pin An; Weng, Yi Lan; Chen, Mei Yu

doi:10.1016/j.bbrc.2007.06.016

Cited by 9 publications

(15 citation statements)

References 25 publications

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“…For this analysis, we defined homologues as genes encoding proteins containing both a GT-8 and a GT49 glycosyltransferase domain. Although the Dictyostelium discoideum genome has been reported to contain LARGE homologues [76], the predicted proteins contain only the GT-8 domain and thus are unlikely to be true orthologues. We were interested to find that the genome of the demosponge Reniera appears to contain a single (intronless) LARGE gene.…”

Section: The Evolution Of Large Genesmentioning

confidence: 99%

Dystroglycan glycosylation and muscular dystrophy

Moore

Hewitt

2008

Glycoconj J

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Dystroglycan is an integral member of the skeletal muscle dystrophin glycoprotein complex, which links dystrophin to proteins in the extracellular matrix. Recently, a group of human muscular dystrophy disorders have been demonstrated to result from defective glycosylation of the alpha-dystroglycan subunit. Genetic studies of these diseases have identified six genes that encode proteins required for the synthesis of essential carbohydrate structures on dystroglycan. Here we highlight their known or postulated functions. This glycosylation pathway appears to be highly specific (dystroglycan is the only substrate identified thus far) and to be highly conserved during evolution.

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Section: The Evolution Of Large Genesmentioning

confidence: 99%

Dystroglycan glycosylation and muscular dystrophy

Moore

Hewitt

2008

Glycoconj J

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“…Moreover, mutations in the LARGE gene are also found in spontaneous myodystrophy myd mouse (Arnold et al 2007;Pang et al 2007;Ruddock and Molinari 2006). They are also associated with human muscular dystrophy (Arnold et al 2007;Pang et al 2007;Ruddock and Molinari 2006). The predicted protein structure of LARGE contains an N-terminal cytoplasmic domain, a transmembrane region, a coiled-coil motif, two putative catalytic domains with the conserved DXD motif typical of many glycosyltransferases, and a structural conserved domain as the glycosyltransferase (Busch et al 1998;Grewal and Hewitt 2002;Hwa et al 2007;Pang et al 2007;Peyrard et al 1999).…”

Section: Introductionmentioning

confidence: 96%

“…It was first identified within a genomic region frequently deleted in human meningioma, a type of brain tumor (Hwa et al 2007;Molinari 2007). Moreover, mutations in the LARGE gene are also found in spontaneous myodystrophy myd mouse (Arnold et al 2007;Pang et al 2007;Ruddock and Molinari 2006). They are also associated with human muscular dystrophy (Arnold et al 2007;Pang et al 2007;Ruddock and Molinari 2006).…”

Section: Introductionmentioning

confidence: 97%

“…They are also associated with human muscular dystrophy (Arnold et al 2007;Pang et al 2007;Ruddock and Molinari 2006). The predicted protein structure of LARGE contains an N-terminal cytoplasmic domain, a transmembrane region, a coiled-coil motif, two putative catalytic domains with the conserved DXD motif typical of many glycosyltransferases, and a structural conserved domain as the glycosyltransferase (Busch et al 1998;Grewal and Hewitt 2002;Hwa et al 2007;Pang et al 2007;Peyrard et al 1999). The proximal catalytic domain is most homologous to a bacterial family, the GT8 glycosyltransferases of the Carbohydrate-Active enZymes (CAZy) database (Coutinho et al 2003).…”

Section: Introductionmentioning

confidence: 98%

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LGTBase: LARGE-like GlcNAc Transferase Database

Hwa

Lin

2011

Soft Comput

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Information technology has greatly speeded up the discovery in biomedical research. However, most of the modern biomedical scientists are not familiar with the new technology. To overcome the difficulty, an intelligent information system is needed to help scientists in designing and conducting research projects. Previously, we have designed a static knowledge management system for the LARGE-like glycosyltransferase, a novel GlcNAc transferase involved in human diseases such as muscular dystrophy and human meningioma, by integrating data from public databases. According the characteristics of protein structure of LARGE protein family members include an N-terminal cytoplasmic domain, a transmembrane region, a coiled-coil motif and a putative catalytic domain with the conserved aspartate-any residue-aspartate motif and a conserved protein structural domain. In this paper, we have described an intelligent information system for the LARGE-like GlcNAc Transferase Database, by setting up an automatic updating databank for genes of the LARGE family and by integrating several bioinformatics tools which can identify characteristics structural domains of the protein family.

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“…Previously, we have identified four genes, gnt12, gnt13, gnt14, and gnt15 from D. discoideum, as GlnNAc-transferase [4]. Our annotation is based on the sequences similarity to human and mouse LARGE proteins based on BLASTP [5].…”

Section: Introductionmentioning

confidence: 99%

Classification of LARGE-liked GlcNAc-Transferases of Dictyostelium discoideum by Phylogenetic Analysis

Hwa

2007

2007 Frontiers in the Convergence of Bioscience and Information Technologies

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GlcNAc transferases are important enzymes involved in protein glycosylation, a cellular process controlling life-time, location and function of proteins. Previously, four new genes in Dictyostelium discoideum through a forward genetic screening, and BLASP search are annotated as gnt12 (GlcNAc Transferase), gnt13, gnt14, and gnt15 since their deduced amino acid sequences share significant similarity to mammalian LARGE, a GlcNAC glycosyltransferase involved on the functional maturation of α-dystroglycan, a key molecule associated with human muscular dystrophy. However, the four genes of Dicystelium are not included in CAZy (Carbohydrate-Active enZymes) database, in which glycosyltransferases were classified based on structural, reaction mechanism and sequence similarities. Here we presented our bioinformatics analysis workflow based on phylogentic analysis to determine if these four genes are in related to the glycosyltransferase 2 and/or 49 families. And, we have also provided the experimental evidence with altered glycosylation pattern in the genetic engineered mutant of gnt 15 -.

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Dictyostelium gnt15 encodes a protein with similarity to LARGE and plays an essential role in development

Cited by 9 publications

References 25 publications

Dystroglycan glycosylation and muscular dystrophy

Dystroglycan glycosylation and muscular dystrophy

LGTBase: LARGE-like GlcNAc Transferase Database

Classification of LARGE-liked GlcNAc-Transferases of Dictyostelium discoideum by Phylogenetic Analysis

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