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The common repeat sequence: aspartate-serine-serine (DSS) or glutamate-serine-serine (ESS), where the serine is often phosphorylated. An example of such proteins we and others have associated with the mineralization process, are the so-called SIBLING proteins: osteopontin [30,71,72,73], dentin matrix protein 1 [33,74,75], matrix extracellular phosphoglycoprotein [76], bone sialoprotein [77,78] and
The common repeat sequence: aspartate-serine-serine (DSS) or glutamate-serine-serine (ESS), where the serine is often phosphorylated. An example of such proteins we and others have associated with the mineralization process, are the so-called SIBLING proteins: osteopontin [30,71,72,73], dentin matrix protein 1 [33,74,75], matrix extracellular phosphoglycoprotein [76], bone sialoprotein [77,78] and
The common repeat sequence: aspartate-serine-serine (DSS) or glutamate-serine-serine (ESS), where the serine is often phosphorylated. An example of such proteins we and others have associated with the mineralization process, are the so-called SIBLING proteins: osteopontin [30,71,72,73], dentin matrix protein 1 [33,74,75], matrix extracellular phosphoglycoprotein [76], bone sialoprotein [77,78] and

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Is promoted by higher temperatures (10). In addition to proteases, the DnaK chaperone system consisting of DnaK (Hsp70), DnaJ (Hsp40), and GrpE (nucleotide exchange factor) is required for the rapid degradation of 32 in vivo because the half-life of 32 is much longer in dnaK, dnaJ, and grpE mutants (11, 12). 32 directly interacts with DnaK or DnaJ and forms a stable ternary complex in the presence
Igure 6 TM domain alignments of SMR proteins with MFS members TM domain alignments of SMR proteins with MFS members. Artificial fusions proteins of all SMR proteins from each subclass were performed (data not shown) and selected alignments for the fused protein pairs Bsu-EbrA to Bsu-EbrB, and EcoEmrE to Eco-SugE are shown with MFS transporters from Pseudomonas aeruginosa (NP_253969; 389 a.a) and f
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Tive substrate, bacteriophage P1 RepA protein, have located DnaK- and DnaJ-binding sites in RepA (25). To gain further insight into chaperone functions in 32 degradation, we isolated many 32 mutants that are stable in vivo (26). These mutants contain one or two amino acid substitutions in the N-terminal half of Region 2.1. In this study, we examined the affinity of some mutant 32 for proteases and
F the IDP domain containing an asparagine and proline (Asn- and Pro)-rich region, with glycine (Gly)- and glutamine (Gln)-rich repeats mid-sequence is implicated in self- assembly. Based on analytical ultracentrifugation, the glycine-rich region oligomerizes to form large protein assemblies. The proline-rich region also shows a self-Author Manuscript Author Manuscript Author Manuscript Author Manu
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F the IDP domain containing an asparagine and proline (Asn- and Pro)-rich region, with glycine (Gly)- and glutamine (Gln)-rich repeats mid-sequence is implicated in self- assembly. Based on analytical ultracentrifugation, the glycine-rich region oligomerizes to form large protein assemblies. The proline-rich region also shows a self-Author Manuscript Author Manuscript Author Manuscript Author Manu
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