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Urochordate serpins are Classified into Six Groups Encoded by Exon-Intron Structures, Microsynteny and Bayesian Phylogenetic Analyses.

Kumar A, Bhandari A - J Genomics (2014)

Bottom Line: The exon/intron structures and genomic locus comparisons together with sequence phylogenetic analysis, suggested that urochordate serpins are classified into six groups (U1-U6), different from six groups (V1-V6) of vertebrate serpins.Human α1-antitrypsin shared lower sequence identities and similarities with urochordates serpins ranged from 14-29% and 30-49%, respectively.Based on protein sequences, genes and genomic architectures, we conclude that these two urochordates do not contain a single copy of genuine ortholog of the vertebrate serpins.

View Article: PubMed Central - PubMed

Affiliation: 1. Department of Genetics & Molecular Biology in Botany, Institute of Botany, Christian-Albrechts-University at Kiel, Kiel, Germany.

ABSTRACT
Members of serpin superfamily are involved in wide array of cellular processes to control proteolytic activities of eukaryotic organisms. Vertebrate serpins are extensively studied and reported to be classified into six groups (V1-V6) based on gene structures. However, there is no study conducted for serpins in urochordates (the closest living invertebrates related to vertebrates) to date. To unravel further the phylogenetic history of serpin genes, we characterized serpin genes from two urochordates (Ciona intestinalis and Ciona savignyi). There are 11 and 5 serpins in the C. intestinalis and C. savignyi, respectively. The exon/intron structures and genomic locus comparisons together with sequence phylogenetic analysis, suggested that urochordate serpins are classified into six groups (U1-U6), different from six groups (V1-V6) of vertebrate serpins. Human α1-antitrypsin shared lower sequence identities and similarities with urochordates serpins ranged from 14-29% and 30-49%, respectively. Based on protein sequences, genes and genomic architectures, we conclude that these two urochordates do not contain a single copy of genuine ortholog of the vertebrate serpins.

No MeSH data available.


Protein structural models of two Ciona serpins. These two protein models are based on the crystal structure of human α1-antitrypsin (PDB Id: 1OPH, chain:A) with RMSD of 0.67 Å and 0.66 Å, respectively.
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Figure 5: Protein structural models of two Ciona serpins. These two protein models are based on the crystal structure of human α1-antitrypsin (PDB Id: 1OPH, chain:A) with RMSD of 0.67 Å and 0.66 Å, respectively.

Mentions: Additionally, homology models of Ci-Spn-9 and Cs-Spn-2 illustrate the conserved serpin core with endoplasmic reticulum retention signals as HDEF and HDEL (Fig. 5), respectively. These two serpins have different RCL sequences.


Urochordate serpins are Classified into Six Groups Encoded by Exon-Intron Structures, Microsynteny and Bayesian Phylogenetic Analyses.

Kumar A, Bhandari A - J Genomics (2014)

Protein structural models of two Ciona serpins. These two protein models are based on the crystal structure of human α1-antitrypsin (PDB Id: 1OPH, chain:A) with RMSD of 0.67 Å and 0.66 Å, respectively.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4150122&req=5

Figure 5: Protein structural models of two Ciona serpins. These two protein models are based on the crystal structure of human α1-antitrypsin (PDB Id: 1OPH, chain:A) with RMSD of 0.67 Å and 0.66 Å, respectively.
Mentions: Additionally, homology models of Ci-Spn-9 and Cs-Spn-2 illustrate the conserved serpin core with endoplasmic reticulum retention signals as HDEF and HDEL (Fig. 5), respectively. These two serpins have different RCL sequences.

Bottom Line: The exon/intron structures and genomic locus comparisons together with sequence phylogenetic analysis, suggested that urochordate serpins are classified into six groups (U1-U6), different from six groups (V1-V6) of vertebrate serpins.Human α1-antitrypsin shared lower sequence identities and similarities with urochordates serpins ranged from 14-29% and 30-49%, respectively.Based on protein sequences, genes and genomic architectures, we conclude that these two urochordates do not contain a single copy of genuine ortholog of the vertebrate serpins.

View Article: PubMed Central - PubMed

Affiliation: 1. Department of Genetics & Molecular Biology in Botany, Institute of Botany, Christian-Albrechts-University at Kiel, Kiel, Germany.

ABSTRACT
Members of serpin superfamily are involved in wide array of cellular processes to control proteolytic activities of eukaryotic organisms. Vertebrate serpins are extensively studied and reported to be classified into six groups (V1-V6) based on gene structures. However, there is no study conducted for serpins in urochordates (the closest living invertebrates related to vertebrates) to date. To unravel further the phylogenetic history of serpin genes, we characterized serpin genes from two urochordates (Ciona intestinalis and Ciona savignyi). There are 11 and 5 serpins in the C. intestinalis and C. savignyi, respectively. The exon/intron structures and genomic locus comparisons together with sequence phylogenetic analysis, suggested that urochordate serpins are classified into six groups (U1-U6), different from six groups (V1-V6) of vertebrate serpins. Human α1-antitrypsin shared lower sequence identities and similarities with urochordates serpins ranged from 14-29% and 30-49%, respectively. Based on protein sequences, genes and genomic architectures, we conclude that these two urochordates do not contain a single copy of genuine ortholog of the vertebrate serpins.

No MeSH data available.