+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Genome-wide survey of prokaryotic serine proteases: analysis of distribution and domain architectures of five serine protease families in prokaryotes

Genome-wide survey of prokaryotic serine proteases: analysis of distribution and domain architectures of five serine protease families in prokaryotes

Bmc Genomics 9: 549

Serine proteases are one of the most abundant groups of proteolytic enzymes found in all the kingdoms of life. While studies have established significant roles for many prokaryotic serine proteases in several physiological processes, such as those associated with metabolism, cell signalling, defense response and development, functional associations for a large number of prokaryotic serine proteases are relatively unknown. Current analysis is aimed at understanding the distribution and probable biological functions of the select serine proteases encoded in representative prokaryotic organisms. A total of 966 putative serine proteases, belonging to five families, were identified in the 91 prokaryotic genomes using various sensitive sequence search techniques. Phylogenetic analysis reveals several species-specific clusters of serine proteases suggesting their possible involvement in organism-specific functions. Atypical phylogenetic associations suggest an important role for lateral gene transfer events in facilitating the widespread distribution of the serine proteases in the prokaryotes. Domain organisations of the gene products were analysed, employing sensitive sequence search methods, to infer their probable biological functions. Trypsin, subtilisin and Lon protease families account for a significant proportion of the multi-domain representatives, while the D-Ala-D-Ala carboxypeptidase and the Clp protease families are mostly single-domain polypeptides in prokaryotes. Regulatory domains for protein interaction, signalling, pathogenesis, cell adhesion etc. were found tethered to the serine protease domains. Some domain combinations (such as S1-PDZ; LON-AAA-S16 etc.) were found to be widespread in the prokaryotic lineages suggesting a critical role in prokaryotes. Domain architectures of many serine proteases and their homologues identified in prokaryotes are very different from those observed in eukaryotes, suggesting distinct roles for serine proteases in prokaryotes. Many domain combinations were found unique to specific prokaryotic species, suggesting functional specialisation in various cellular and physiological processes.

Please choose payment method:

(PDF emailed within 0-6 h: $19.90)

Accession: 053397823

Download citation: RISBibTeXText

PMID: 19019219

DOI: 10.1186/1471-2164-9-549

Related references

Expression and localization of the serine proteases high-temperature requirement factor A1, serine protease 23, and serine protease 35 in the mouse ovary. Endocrinology 149(10): 5070-5077, 2008

Evolutionary genomics of Glossina morsitans immune-related CLIP domain serine proteases and serine protease inhibitors. Infection Genetics and Evolution 11(4): 740-745, 2011

Two clip domain family of serine proteases and a serine protease homolog from the fall webworm, Hyphantria cunea; cDNA cloning and characterization. Entomological Research Seoul 34(4): 253-260, 2004

Three clip domain serine proteases (cSPs) and one clip domain serine protease homologue (cSPH) identified from haemocytes and eyestalk cDNA libraries of swimming crab Portunus trituberculatus. Fish & Shellfish Immunology 32(4): 565-571, 2012

Current genome-wide analysis on serine proteases in innate immunity. Current Genomics 5(2): 147-155, 2004

Genome-wide identification, domain architectures and phylogenetic analysis provide new insights into the early evolution of shikimate pathway in prokaryotes. Molecular Phylogenetics and Evolution 75: 154-164, 2014

Serine proteases, serine protease inhibitors, and protease-activated receptors: roles in synaptic function and behavior. Brain Research 1407: 107-122, 2011

Prokaryotic expression, purification and activity analysis of recombinant human serine protease inhibitor Hespintor Kazal Domain. Sheng Wu Gong Cheng Xue Bao 29(11): 1607-1616, 2013

Vacuolar proteases from Candida glabrata: Acid aspartic protease PrA, neutral serine protease PrB and serine carboxypeptidase CpY. The nitrogen source influences their level of expression. Revista Iberoamericana de Micologia 33(1): 26-33, 2016

Genome-wide identification and expression analysis of serine proteases and homologs in the silkworm Bombyx mori. Bmc Genomics 11: 405, 2010

Amblyomma americanum tick saliva serine protease inhibitor 6 is a cross-class inhibitor of serine proteases and papain-like cysteine proteases that delays plasma clotting and inhibits platelet aggregation. Insect Molecular Biology 22(3): 306-319, 2013

Serine proteases and serine protease inhibitors in testicular physiology: the plasminogen activation system. Reproduction 134(6): 721-729, 2007

Regulation of renal sodium handling through the interaction between serine proteases and serine protease inhibitors. Clinical and Experimental Nephrology 14(5): 405-410, 2010

The role of serine proteases and serine protease inhibitors in the migration of gonadotropin-releasing hormone neurons. BMC Developmental Biology 2(1 Cited April ): 1-11, 2002

Intracellular serine protease from Bacillus subtilis. Structural comparison with extracellular serine proteases-subtilisins. Biochemical and Biophysical Research Communications 77(1): 298-305, 1977