Vertebrate serpins: construction of a conflict-free phylogeny by combining exon-intron and diagnostic site analyses - PubMed (original) (raw)
Vertebrate serpins: construction of a conflict-free phylogeny by combining exon-intron and diagnostic site analyses
H Ragg et al. Mol Biol Evol. 2001 Apr.
Abstract
A combination of three independent biological features, genomic organization, diagnostic amino acid sites, and rare indels, was used to elucidate the phylogeny of the vertebrate serpin (serine protease inhibitor) superfamily. A strong correlation between serpin gene families displaying (1) a conserved exon-intron pattern and (2) family-specific combinations of amino acid residues at specific sites suggests that present-day vertebrates encompass six serpin gene families which evolved from primordial genes by massive intron insertion before or during early vertebrate radiation. Introns placed at homologous positions in the gene sequences in combination with diagnostic sequence characters may also constitute a reliable kinship indicator for other protein superfamilies.
Similar articles
- Isolation and characterization of a novel serine protease inhibitor, SjSPI, from Schistosoma japonicum.
Zhang Y, Guo J, He L, Zong HY, Cai GB. Zhang Y, et al. Parasitol Int. 2018 Aug;67(4):415-424. doi: 10.1016/j.parint.2018.04.002. Epub 2018 Apr 9. Parasitol Int. 2018. PMID: 29649563 - Ixodes scapularis tick serine proteinase inhibitor (serpin) gene family; annotation and transcriptional analysis.
Mulenga A, Khumthong R, Chalaire KC. Mulenga A, et al. BMC Genomics. 2009 May 12;10:217. doi: 10.1186/1471-2164-10-217. BMC Genomics. 2009. PMID: 19435496 Free PMC article. - The role of serpins in vertebrate immunity.
Mangan MS, Kaiserman D, Bird PI. Mangan MS, et al. Tissue Antigens. 2008 Jul;72(1):1-10. doi: 10.1111/j.1399-0039.2008.01059.x. Epub 2008 May 20. Tissue Antigens. 2008. PMID: 18498291 Review. - Human clade B serpins (ov-serpins) belong to a cohort of evolutionarily dispersed intracellular proteinase inhibitor clades that protect cells from promiscuous proteolysis.
Silverman GA, Whisstock JC, Askew DJ, Pak SC, Luke CJ, Cataltepe S, Irving JA, Bird PI. Silverman GA, et al. Cell Mol Life Sci. 2004 Feb;61(3):301-25. doi: 10.1007/s00018-003-3240-3. Cell Mol Life Sci. 2004. PMID: 14770295 Free PMC article. Review.
Cited by
- Origin and diversification of the plasminogen activation system among chordates.
Chana-Muñoz A, Jendroszek A, Sønnichsen M, Wang T, Ploug M, Jensen JK, Andreasen PA, Bendixen C, Panitz F. Chana-Muñoz A, et al. BMC Evol Biol. 2019 Jan 17;19(1):27. doi: 10.1186/s12862-019-1353-z. BMC Evol Biol. 2019. PMID: 30654737 Free PMC article. - Probing the folding pathway of a consensus serpin using single tryptophan mutants.
Yang L, Irving JA, Dai W, Aguilar MI, Bottomley SP. Yang L, et al. Sci Rep. 2018 Feb 1;8(1):2121. doi: 10.1038/s41598-018-19567-9. Sci Rep. 2018. PMID: 29391487 Free PMC article. - Expression of SERPINA3s in cattle: focus on bovSERPINA3-7 reveals specific involvement in skeletal muscle.
Péré-Brissaud A, Blanchet X, Delourme D, Pélissier P, Forestier L, Delavaud A, Duprat N, Picard B, Maftah A, Brémaud L. Péré-Brissaud A, et al. Open Biol. 2015 Sep;5(9):150071. doi: 10.1098/rsob.150071. Open Biol. 2015. PMID: 26562931 Free PMC article. - Origin of serpin-mediated regulation of coagulation and blood pressure.
Wang Y, Köster K, Lummer M, Ragg H. Wang Y, et al. PLoS One. 2014 May 19;9(5):e97879. doi: 10.1371/journal.pone.0097879. eCollection 2014. PLoS One. 2014. PMID: 24840053 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources