alexa Comparative and Evolutionary Studies of Vertebrate Extr
ISSN: 0974-276X

Journal of Proteomics & Bioinformatics
Open Access

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Research Article

Comparative and Evolutionary Studies of Vertebrate Extracellular Sulfatase Genes and Proteins: SULF1 and SULF2

Roger S Holmes*

Griffith Institute for Drug Discovery and School of Natural Sciences, Griffith University, Nathan, QLD, Australia

*Corresponding Author:
Roger S Holmes
Emeritus Professor
Griffith Institute for Drug Discovery and School of Natural Sciences
Griffith University, Nathan, QLD, 4111 Australia
Tel: 61-410-583-348
E-mail: [email protected]

Received Date: January 10, 2017; Accepted Date: February 02, 2017; Published Date: February 16, 2017

Citation: Holmes RS (2017) Comparative and Evolutionary Studies of Vertebrate Extracellular Sulfatase Genes and Proteins: SULF1 and SULF2. J Proteomics Bioinform 10:32-40. doi: 10.4172/jpb.1000423

Copyright: © 2017 Holmes RS. 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

Extracellular sulfatases (SULF1; SULF2) (EC: 3.1.6.-) are members of the sulfatase enzyme family which exhibit endoglucosamine-6-sulfatase activity and carry out essential roles in proteoglycan metabolism. These enzymes regulate a number of critical signalling pathways and the sulfation state of glycoaminoglycans in the extracellular space. SULF1 and SULF2 amino acid sequences and structures and SULF-like gene locations were examined using bioinformatic data from several genome projects. Sequence alignments and conserved secondary structures and key amino acid residues and domains were studied. Comparative genomic analyses were conducted using the UC Santa Cruz Genome Browser. Phylogeny studies investigated the evolutionary relationships of these genes and proteins. Human and other vertebrate SULF1 and SULF2 sequences were conserved, including signal peptides, metal (Ca2+) and substrate binding sequences, active site residues and N-glycosylation sites (sulfatase domain); and a C-terminal positively charged hydrophilic domain. Predicted 2D structures were identified for the sulfatase domain of vertebrate SULF1 and SULF2 using a bacterial phosphatase structure (PDB:4UPK). Vertebrate SULF1 and SULF2 genes usually contained 18/19 or 20 coding exons, respectively. Transcription factor binding sites and miR-binding sites were identified within the human SULF1 and SULF2 gene promoters and 3’-UTR regions, respectively. The Estrogen Receptor Gene (ESR1) was identified in the SULF2 promoter which may contribute to the higher expression level for this gene in female reproductive tissues. SULF1 and SULF2 genes and proteins were present in all vertebrate genomes examined. Phylogenetic analyses suggested that an ancestral invertebrate SUL1 gene underwent a gene duplication event to form two separate lines of vertebrate gene evolution: SULF1 and SULF2.

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