Proteases: Evolution

Christopher Southan, Oxford GlycoSciences Ltd, Abingdon, UK

Published online: May 2008

DOI: 10.1002/9780470015902.a0006141.pub2

Human proteases have diverse fold structures, catalytic mechanisms, biochemical functions and evolutionary origins. Most arose by gene duplication, but some arose by horizontal transfer from prokaryotes. Adaptation and diversification of their biological roles have resulted from shifts in substrate specificities, expression patterns and new domain combinations.

Keywords: protease; evolution; gene duplication; domains; structure

Figure 1. (a) Phylogram of HtrA proteases. (b) Human HtrA1 Q92743 domain and gene structure. (c) Human HtrA2 O43464 domain and gene structure. kb: kilobases; Mb: megabases.
close
 References
    Apweiler R, Attwood TK, Bairoch A et al. (2000) InterPro – an integrated documentation resource for protein families, domains and functional sites. Bioinformatics 16: 1145–1150.
    Aravind L and Koonin EV (2002) Classification of the caspase-hemoglobinase fold: detection of new families and implications for the origin of the eukaryotic separins. Proteins 46: 355–367.
    Barrett AJ and Rawlings ND (2001) Evolutionary lines of cysteine peptidases. Biological Chemistry 382: 727–733.
    Coates D, Siviter R and Isaac RE (2000) Exploring the Caenorhabditis elegans and Drosophila melanogaster genomes to understand neuropeptide and peptidase function. Biochemical Society Transactions 28: 464–469.
    Crackower MA, Sarao R, Oudit GY et al. (2002) Angiotensin-converting enzyme 2 is an essential regulator of heart function. Nature 417: 822–828.
    Dehal P, Predki P, Olsen AS et al. (2001) Human chromosome 19 and related regions in mouse: conservative and lineage-specific evolution. Science 293: 104–111.
    Fagan R, Swindells M, Overington J and Weir M (2001) Nicastrin, a presenilin-interacting protein, contains an aminopeptidase/transferrin receptor superfamily domain. Trends in Biochemical Sciences 26: 213–214.
    Gibson TJ and Spring J (2000) Evidence in favour of ancient octaploidy in the vertebrate genome. Biochemical Society Transactions 28: 259–264.
    Koc EC, Burkhart W, Blackburn K et al. (2001) The large subunit of the mammalian mitochondrial ribosome. Analysis of the complement of ribosomal proteins present. Journal of Biological Chemistry 276: 43958–43969.
    Krem MM and Di Cera E (2001) Molecular markers of serine protease evolution. EMBO Journal 20: 3036–3045.
    Krojer T, Garrido-Franco M, Huber R, Ehrmann M and Clausen T (2002) Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine. Nature 416: 455–459.
    Pallen MJ and Wren BW (1997) The HtrA family of serine proteases. Molecular Microbiology 26: 209–221.
    Ponting CP (1997) Evidence for PDZ domains in bacteria, yeast, and plants. Protein Science 6: 464–468.
    Rawlings ND, O'Brien E and Barrett AJ (2002) MEROPS: the protease database. Nucleic Acids Research 30: 343–346.
    Smith TS, Southan C, Ellington K et al. (2001) Identification, genomic organization, and mRNA expression of LACTB, encoding a serine -lactamase-like protein with an amino-terminal transmembrane domain. Genomics 78: 12–14.
    Southan C (2000) Website review: InterPro (the integrated resource of protein domains and functional sites). Yeast 17: 327–334.
 Further Reading
    Clausen T, Southan C and Ehrmann M (2002) The HtrA family of proteases. Implications for protein composition and cell fate. Molecular Cell 10(3): 443–455.
    Gerlt JA and Babbitt PC (2001) Divergent evolution of enzymatic function: mechanistically diverse superfamilies and functionally distinct suprafamilies. Annual Review of Biochemistry 70: 209–246.
    Kageyama T (2002) Pepsinogens, progastricsins, and prochymosins: structure, function, evolution, and development. Cellular and Molecular Life Sciences 59: 288–306.
    Koonin EV and Aravind L (2002) Origin and evolution of eukaryotic apoptosis: the bacterial connection. Cell Death and Differentiation 9: 394–404.
    Krem MM and Cera ED (2002) Evolution of enzyme cascades from embryonic development to blood coagulation. Trends in Biochemical Sciences 27: 67–74.
    Massova I, Kotra LP, Fridman R and Mobashery S (1998) Matrix metalloproteinases: structures, evolution, and diversification. FASEB Journal 12: 1075–1095.
    Patthy L (1999) Genome evolution and the evolution of exon-shuffling – a review. Gene 238: 103–114.
    Ponting CP and Russell RR (2002) The natural history of protein domains. Annual Review of Biophysics and Biomolecular Structure 31: 45–71.
    Southan C (2001) A genomic perspective on human proteases. FEBS Letters 498: 214–218.
    Southan C (2007) Exploiting new genome data and Internet resources for the phylogenetic analysis of proteases, substrates and inhibitors. Biochemical Society Transactions 35: 599–603.
    Volker C and Lupas AN (2002) Molecular evolution of proteasomes. Current Topics in Microbiology and Immunology 268: 1–22.
    Yousef GM and Diamandis EP (2001) The new human tissue kallikrein gene family: structure, function, and association to disease. Endocrine Reviews 22: 184–204.
 Web Links
    ePath European Bioinformatics Institute InterPro database. A resource for whole-genome analysis http://www.ebi.ac.uk/interpro/
    ePath MEROPS Protease Database. A catalog and structure-based classification of proteases, with additional information about them http://merops.sanger.ac.uk

Related Sub-Topics:

Molecular Evolution | Protein Evolution | Evolution of Coding and Functional Modules
Contact Editor close
Submit a note to the editor about this article by filling in the form below.

* Required Field

Article Title: Proteases: Evolution
 
How to Cite close
Southan, Christopher(May 2008) Proteases: Evolution. In: eLS. John Wiley & Sons Ltd, Chichester. http://www.els.net [doi: 10.1002/9780470015902.a0006141.pub2]