Llagen-like proteins in bacteria and that they can type triple-helix structures
Llagen-like proteins in bacteria and that they will kind triple-helix structures even though they lack Hyp (Table 1). In 2000, two proteins inside the gram negative bacterium Streptococcus pyogenes have been discovered to include a substantial length of (Gly-Xaa-Yaa)n amino acid sequence and it was postulated that these type collagenous structures (Lukomski et al. 2000; Rasmussen et al. 2000). As growing numbers of genomic sequences were getting reported, an analysis was carried out on 136 eubacterial genomes (Rasmussen et al. 2003), searching for sequences with homology to (Gly-Pro-Pro)n. Hits have been found for 56 proteins in 25 bacterial genomes, with none noticed in any of the 15 archeobacterial genomes. The HSP40 Source number of Gly-Xaa-Yaa tripeptides varied from 7 to 745, with an typical length of 76 triplets, and these collagenlike sequences are generally flanked by non-collagenous domains. The collagen-like sequences from various bacteria all had a comparatively higher Pro content, and Rasmussen et al. (2003) identified distinctive amino acid compositions for various prospective proteins which could be categorized as Thr-rich, Pro-rich, or rich in charged residues. Pro was preferentially found in the X position in bacterial proteins in contrast to mammalian collagens exactly where you will find usually half or far more from the Pro residues within the Yaa-position, that are subsequently hydroxylated. Conversely, within the bacterial collagens Thr and Gln are considerably more frequent in the Yaa-position than observed for mammalian collagens (Rasmussen et al. 2003). Several bacterial genomes contained a number of collagen-like sequences, as much as 9 in some circumstances, so it’s doable that heterotrimers, with two or three unique chains, are formed in these instances. It has been suggested that bacterial collagen sequences arise from horizontal gene transfer from eukaryotes to bacteria (Rasmussen et al. 2003). Clearly, inside the ten years due to the fact this initial study was reported, the extent in the genomic info has elevated many-fold along with a huge number of more genomes are available for interrogation. Additional studies on quite a few of these bacterial proteins have confirmed that they have the characteristic triple-helix structure of collagen and suggest they may play critical roles in pathogenesis. These proteins, which are getting recognized in growing numbers, are no longer unexpected curiosities, but represent an opportunity for approaching basic science CYP11 Purity & Documentation troubles in collagen and for biomaterial applications.NIH-PA Author Manuscript NIH-PA Author Manuscript NIH-PA Author ManuscriptJ Struct Biol. Author manuscript; obtainable in PMC 2015 June 01.Yu et al.Page2. Biological role of bacterial collagen-like proteinsWhile there are numerous bacterial species that include collagen-like sequences within the genome (Rasmussen et al. 2003), there’s evidence for their organic expression for only several situations (Karlstrom et al. 2004; 2006). A few pathogenic bacterial systems have been properly characterized and these instances suggest the collagen protein may interact with all the host to assist invasion or assist a pathogen evade the host immune system. The two S. pyogenes bacterial collagens, Scl1 and Scl2, have sequences indicating they’re anchored on the cell surface and have already been shown to bind to many different host proteins. Based around the precise serotype, the non-collagenous V-domain of Scl1 may bind to high-density lipoprotein (HDL) (Gao et al. 2010), low-density lipoprotein (LDL) (Han et al. 2006a), factor H (Caswell et al. 2008a),.