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Exosortase
Exosortase refers to a family of integral membrane proteins that occur in Gram-negative bacteria that recognizes and cleaves the carboxyl-terminal protein targeting, sorting signal PEP-CTERM. The name derives from a predicted role analogous to sortase, despite the lack of any detectable sequence homology, and a strong association of exosortase genes with exopolysaccharide or extracellular polymeric substance biosynthesis loci. Many archaea have an archaeosortase, homologous to exosortases rather than to sortases. Archaeosortase A recognizes the signal PGF-CTERM, found at the C-terminus of some archaeal S-layer proteins. Following processing by archaeosortase A, the PGF-CTERM region is gone, and a prenyl-derived lipid anchor is present at the C-terminus instead. Exosortase has not itself been characterized biochemically. However, site-directed mutagenesis work on archaeosortase A, an archaeal homolog of exosortases, strongly supports the notion of a cysteine, Cys active site and co ...
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Archaeosortase
An archaeosortase is a protein that occurs in the cell membranes of some archaea. Archaeosortases recognize and remove carboxyl-terminal protein targeting, protein sorting signals about 25 amino acids long from secreted proteins. A genome that encodes one archaeosortase may encode over fifty target proteins. The best characterized archaeosortase target is the Haloferax volcanii S-layer glycoprotein, an extensively modified protein with O-linked glycosylation, O-linked glycosylations, N-linked glycosylation, N-linked glycosylations, and a large prenyl-derived prenylation, lipid modification toward the C-terminus. Knockout of the archaeosortase A (artA) gene, or permutation of the motif Pro-Gly-Phe (PGF) to Pro-Phe-Gly in the S-layer glycoprotein, blocks attachment of the lipid moiety as well as blocking removal of the PGF-CTERM protein-sorting domain. Thus archaeosortase appears to be a wikt:transpeptidase, transpeptidase, like sortase, rather than a simple protease. Archaeosortases ...
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Gram-negative Bacteria
Gram-negative bacteria are bacteria that, unlike gram-positive bacteria, do not retain the Crystal violet, crystal violet stain used in the Gram staining method of bacterial differentiation. Their defining characteristic is that their cell envelope consists of a thin peptidoglycan gram-negative cell wall, cell wall sandwiched between an inner (Cytoplasm, cytoplasmic) Cell membrane, membrane and an Bacterial outer membrane, outer membrane. These bacteria are found in all environments that support life on Earth. Within this category, notable species include the model organism ''Escherichia coli'', along with various pathogenic bacteria, such as ''Pseudomonas aeruginosa'', ''Chlamydia trachomatis'', and ''Yersinia pestis''. They pose significant challenges in the medical field due to their outer membrane, which acts as a protective barrier against numerous Antibiotic, antibiotics (including penicillin), Detergent, detergents that would normally damage the inner cell membrane, and the ...
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Protein Targeting
Protein targeting or protein sorting is the biological mechanism by which proteins are transported to their appropriate destinations within or outside the cell. Proteins can be targeted to the inner space of an organelle, different intracellular membranes, the plasma membrane, or to the exterior of the cell via secretion. Information contained in the protein itself directs this delivery process. Correct sorting is crucial for the cell; errors or dysfunction in sorting have been linked to multiple diseases. History In 1970, Günter Blobel conducted experiments on protein translocation across membranes. Blobel, then an assistant professor at Rockefeller University, built upon the work of his colleague George Palade. Palade had previously demonstrated that non-secreted proteins were translated by free ribosomes in the cytosol, while secreted proteins (and target proteins, in general) were translated by ribosomes bound to the endoplasmic reticulum (ER). Candidate explanations at t ...
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Sortase
Sortase refers to a group of prokaryotic enzymes that modify surface proteins by recognizing and cleaving a carboxyl-terminal sorting signal. For most substrates of sortase enzymes, the recognition signal consists of the motif LPXTG (Leu-Pro-any-Thr-Gly), then a highly hydrophobic transmembrane sequence, followed by a cluster of basic residues such as arginine. Cleavage occurs between the Thr and Gly, with transient attachment through the Thr residue to the active site Cys residue, followed by transpeptidation that attaches the protein covalently to cell wall components. Sortases occur in almost all Gram-positive bacteria and the occasional Gram-negative bacterium (e.g. '' Shewanella putrefaciens'') or Archaea (e.g. '' Methanobacterium thermoautotrophicum''), where cell wall LPXTG-mediated decoration has not been reported. Although sortase A, the "housekeeping" sortase, typically acts on many protein targets, other forms of sortase recognize variant forms of the cleavage motif, ...
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Sequence Homology
Sequence homology is the homology (biology), biological homology between DNA sequence, DNA, RNA sequence, RNA, or Protein primary structure, protein sequences, defined in terms of shared ancestry in the evolutionary history of life. Two segments of DNA can have shared ancestry because of three phenomena: either a speciation event (orthologs), or a Gene duplication, duplication event (paralogs), or else a Horizontal gene transfer, horizontal (or lateral) gene transfer event (xenologs). Homology among DNA, RNA, or proteins is typically inferred from their nucleotide or amino acid sequence similarity. Significant similarity is strong evidence that two sequences are related by evolutionary changes from a common ancestral sequence. Sequence alignment, Alignments of multiple sequences are used to indicate which regions of each sequence are homologous. Identity, similarity, and conservation The term "percent homology" is often used to mean "sequence similarity”, that is the percen ...
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Exopolysaccharide
Extracellular polymeric substances (EPS) are natural polymers of high molecular weight secreted by microorganisms into their environment. EPS establish the functional and structural integrity of biofilms, and are considered the fundamental component that determines the physicochemical properties of a biofilm. EPS in the matrix of biofilms provides compositional support and protection of microbial communities from the harsh environments. Components of EPS can be of different classes of polysaccharides, lipids, nucleic acids, proteins, lipopolysaccharides, and minerals. Components EPS are mostly composed of polysaccharides (exopolysaccharides) and proteins, but include other macromolecules such as DNA, lipids and humic substances. EPS are the construction material of bacterial settlements and either remain attached to the cell's outer surface, or are secreted into its growth medium. These compounds are important in biofilm formation and cells' attachment to surfaces. EPS constit ...
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Extracellular Polymeric Substance
Extracellular polymeric substances (EPS) are biopolymer, natural polymers of molecular mass, high molecular weight secreted by microorganisms into their environment. EPS establish the functional and structural integrity of biofilms, and are considered the fundamental component that determines the physicochemical properties of a biofilm. EPS in the matrix of biofilms provides compositional support and protection of microbial communities from the harsh environments. Components of EPS can be of different classes of polysaccharides, lipids, nucleic acids, proteins, lipopolysaccharides, and minerals. Components EPS are mostly composed of polysaccharides (exopolysaccharides) and proteins, but include other macromolecules such as DNA, lipids and Humic acid, humic substances. EPS are the construction material of bacterial settlements and either remain attached to the cell's outer surface, or are secreted into its growth medium. These compounds are important in biofilm formation and cells ...
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Archaea
Archaea ( ) is a Domain (biology), domain of organisms. Traditionally, Archaea only included its Prokaryote, prokaryotic members, but this has since been found to be paraphyletic, as eukaryotes are known to have evolved from archaea. Even though the domain Archaea Cladistics, cladistically includes eukaryotes, the term "archaea" (: archaeon , from the Greek "ἀρχαῖον", which means ancient) in English still generally refers specifically to prokaryotic members of Archaea. Archaea were initially Taxonomy (biology), classified as bacteria, receiving the name archaebacteria (, in the Archaebacteria Kingdom (biology), kingdom), but this term has fallen out of use. Archaeal cells have unique properties separating them from Bacteria and Eukaryote, Eukaryota. Archaea are further divided into multiple recognized phylum, phyla. Classification is difficult because most have not been Isolation (microbiology), isolated in a laboratory and have been detected only by their Gene, gene s ...
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S-layer
An S-layer (surface layer) is a part of the cell envelope found in almost all archaea, as well as in many types of bacteria. The S-layers of both archaea and bacteria consists of a Monolayer, monomolecular layer composed of only one (or, in a few cases, two) identical proteins or glycoproteins. This structure is built via self-assembly and encloses the whole cell surface. Thus, the S-layer protein can represent up to 15% of the whole protein content of a cell. S-layer proteins are poorly conserved or not conserved at all, and can differ markedly even between related species. Depending on species, the S-layers have a thickness between 5 and 25 nm and possess identical pores 2–8 nm in diameter. The terminology "S-layer" was used the first time in 1976. The general use was accepted at the "First International Workshop on Crystalline Bacterial Cell Surface Layers, Vienna (Austria)" in 1984, and in the year 1987 S-layers were defined at the European Molecular Biology Organiz ...
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Cysteine
Cysteine (; symbol Cys or C) is a semiessential proteinogenic amino acid with the chemical formula, formula . The thiol side chain in cysteine enables the formation of Disulfide, disulfide bonds, and often participates in enzymatic reactions as a nucleophile. Cysteine is chiral, but both D and L-cysteine are found in nature. LCysteine is a protein monomer in all biota, and D-cysteine acts as a signaling molecule in mammalian nervous systems. Cysteine is named after its discovery in urine, which comes from the urinary bladder or cyst, from Ancient Greek, Greek κύστις ''kýstis'', "bladder". The thiol is susceptible to oxidation to give the disulfide bond, disulfide derivative cystine, which serves an important structural role in many proteins. In this case, the symbol Cyx is sometimes used. The deprotonated form can generally be described by the symbol Cym as well. When used as a food additive, cysteine has the E number E920. Cysteine is Genetic code, encoded by the codo ...
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Convergent Evolution
Convergent evolution is the independent evolution of similar features in species of different periods or epochs in time. Convergent evolution creates analogous structures that have similar form or function but were not present in the last common ancestor of those groups. The cladistic term for the same phenomenon is Cladogram#Homoplasies, homoplasy. The recurrent evolution of flight is a classic example, as flying pterygota, insects, birds, pterosaurs, and bats have independently evolved the useful capacity of flight. Functionally similar features that have arisen through convergent evolution are ''analogous'', whereas ''homology (biology), homologous'' structures or traits have a common origin but can have dissimilar functions. Bird, bat, and pterosaur wings are analogous structures, but their forelimbs are homologous, sharing an ancestral state despite serving different functions. The opposite of convergence is divergent evolution, where related species evolve different trai ...
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Protein-sorting Transpeptidase
A protein-sorting transpeptidase is an enzyme, such as the sortase SrtA of Staphylococcus aureus, that cleaves one or more target proteins produced by the same cell, as part of a specialized pathway of protein targeting. The typical prokaryotic protein-sorting transpeptidase is characterized as a protease, but does not simply hydrolyze a peptide bond. Instead, the larger, N-terminal portion of the cleaved polypeptide is transferred onto another molecule, such as a precursor of the peptidoglycan cell wall in Gram-positive bacteria. The term sortase is properly reserved for the set of cysteine protease enzymes sortase A, sortase B, and members of additional classes, all of which share homology. However, a growing number of additional protein sorting systems has been described in prokaryotes, involving sorting enzymes that lack any homology to sortase and that appear to have arisen separately by convergent evolution. Although the sortases are the best described members of the protein- ...
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