title: Matrix metalloproteinases outside vertebrates.
abstract: The matrix metalloproteinase (MMP) family belongs to the metzincin clan of zinc-dependent metallopeptidases. Due to their enormous implications in physiology and disease, MMPs have mainly been studied in vertebrates. They are engaged in extracellular protein processing and degradation, and present extensive paralogy, with 23 forms in humans. One characteristic of MMPs is a ~165-residue catalytic domain (CD), which has been structurally studied for 14 MMPs from human, mouse, rat, pig and the oral-microbiome bacterium Tannerella forsythia. These studies revealed close overall coincidence and characteristic structural features, which distinguish MMPs from other metzincins and give rise to a sequence pattern for their identification. Here, we reviewed the literature available on MMPs outside vertebrates and performed database searches for potential MMP CDs in invertebrates, plants, fungi, viruses, protists, archaea and bacteria. These and previous results revealed that MMPs are widely present in several copies in Eumetazoa and higher plants (Tracheophyta), but have just token presence in eukaryotic algae. A few dozen sequences were found in Ascomycota (within fungi) and in double-stranded DNA viruses infecting invertebrates (within viruses). In contrast, a few hundred sequences were found in archaea and >1000 in bacteria, with several copies for some species. Most of the archaeal and bacterial phyla containing potential MMPs are present in human oral and gut microbiomes. Overall, MMP-like sequences are present across all kingdoms of life, but their asymmetric distribution contradicts the vertical descent model from a eubacterial or archaeal ancestor. This article is part of a Special Issue entitled: Matrix Metalloproteinases edited by Rafael Fridman.
authors.affiliation: Proteolysis Lab, Structural Biology Unit, "María-de-Maeztu" Unit of Excellence, Molecular Biology Institute of Barcelona (CSIC), Barcelona Science Park; c/Baldiri Reixac, 15-21, 08028, Barcelona, Spain.
authors.forename: Laura
authors.initials: L
authors.lastname: Marino-Puertas
authors.affiliation: Proteolysis Lab, Structural Biology Unit, "María-de-Maeztu" Unit of Excellence, Molecular Biology Institute of Barcelona (CSIC), Barcelona Science Park; c/Baldiri Reixac, 15-21, 08028, Barcelona, Spain.. Electronic address: thgcri@ibmb.csic.es.
authors.forename: Theodoros
authors.initials: T
authors.lastname: Goulas
authors.affiliation: Proteolysis Lab, Structural Biology Unit, "María-de-Maeztu" Unit of Excellence, Molecular Biology Institute of Barcelona (CSIC), Barcelona Science Park; c/Baldiri Reixac, 15-21, 08028, Barcelona, Spain.. Electronic address: xgrcri@ibmb.csic.es.
authors.forename: F Xavier
authors.initials: FX
authors.lastname: Gomis-Rüth
mesh_terms: D000818:Animals; D001105:Archaea / Q000201:enzymology*; D019843:Archaeal Proteins / Q000737:chemistry / Q000378:metabolism; D001419:Bacteria / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D007448:Invertebrates / Q000201:enzymology*; D020782:Matrix Metalloproteinases / Q000737:chemistry / Q000378:metabolism; D014764:Viral Proteins / Q000737:chemistry / Q000378:metabolism; D014780:Viruses / Q000201:enzymology*
chemical_list: D019843:Archaeal Proteins; D001426:Bacterial Proteins; D014764:Viral Proteins; D020782:Matrix Metalloproteinases
keywords: Catalytic domain; Invertebrates; MMP; Metzincin; Structure-based sequence motif; Zinc metalloproteinase