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首页> 外文期刊>Journal of bacteriology >Isolation of a Periplasmic Molecular Chaperone-Like Protein of Rhodobacter sphaeroides f. sp.denitrificans That Is Homologous to the Dipeptide Transport Protein DppA of Escherichia coli
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Isolation of a Periplasmic Molecular Chaperone-Like Protein of Rhodobacter sphaeroides f. sp.denitrificans That Is Homologous to the Dipeptide Transport Protein DppA of Escherichia coli

机译:球形红球菌分子质类似分子伴侣蛋白的分离f。与大肠杆菌的二肽转运蛋白DppA同源的sp.denitrificans

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A periplasmic protein has been found to prevent aggregation of the acid-unfolded dimethyl sulfoxide reductase (DMSOR), the periplasmic terminal reductase of dimethyl sulfoxide respiration in the phototrophRhodobacter sphaeroides f. sp. denitrificans, in a manner similar to that of the Escherichia colichaperonin GroEL (Matsuzaki et al., Plant Cell Physiol. 37:333–339, 1996). The protein was isolated from the periplasm of the phototroph. It had a molecular mass of 58 kDa and had no subunits. The sequence of 14 amino-terminal residues of the protein was completely identical to that of the periplasmic dipeptide transport protein (DppA) of E. coli. The 58-kDa protein prevented aggregation to a degree comparable to that of GroEL on the basis of monomer protein. The 58-kDa protein also decreased aggregation of guanidine hydrochloride-denatured rhodanese, a mitochondrial matrix protein, during its refolding upon dilution. The 58-kDa protein is a kind of molecular chaperone and could be involved in maintaining unfolded DMSOR, after secretion of the latter into the periplasm, in a competent form for its correct folding.
机译:已发现一种周质蛋白可防止光解型球形红细菌Rhodobacter sphaeroides f中酸未折叠的二甲基亚砜还原酶(DMSOR)的聚集。 sp。 denitrificans ,其表达方式与大肠埃希菌伴侣蛋白GroEL相似(Matsuzaki等人,Plant Cell Physiol。37:333-339,1996)。从光养生物的周质中分离出该蛋白质。它的分子量为58 kDa,没有亚基。该蛋白质的14个氨基末端残基的序列与 E的周质二肽转运蛋白(DppA)的序列完全相同。大肠杆菌。 58-kDa的蛋白质在单体蛋白质的基础上阻止了与GroEL相当程度的聚集。 58 kDa的蛋白质在稀释后重折叠的过程中,还降低了盐酸胍变性的罗丹花(一种线粒体基质蛋白)的聚集。 58 kDa蛋白是一种分子伴侣蛋白,可参与将未折叠的DMSOR分泌到周质中后以维持其正确折叠的有效形式来维持其展开。

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