Detection of a Compact Folding Intermediate of Dimethyl Sulfoxide Reductase Secreted from a Molybdenum Cofactor-Deficient Mutant of Rhodobacter sphaeroides f. sp. denitrificans
Detection of a Compact Folding Intermediate of Dimethyl Sulfoxide Reductase Secreted from a Molybdenum Cofactor-Deficient Mutant of Rhodobacter sphaeroides f. sp. denitrificans
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球形红杆菌 f 钼辅因子缺陷突变体分泌的二甲亚砜还原酶紧凑折叠中间体的检测。
DOI：
10.1093/oxfordjournals.pcp.a029118
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发表时间：
1997
影响因子：
4.9
通讯作者：
T. Satoh
中科院分区：
文献类型：
--
作者：
M. Matsuzaki;T. Satoh
二甲基亚砜还原酶（OMSOR）中的所有九个半胱氨酸残基都以还原巯基形式存在。未折叠的形式，这是以前检测到的DMSOR蛋白分泌的原生质球制备的钼辅因子缺陷型突变体，也检测到从野生型菌株的原生质球时，碘乙酰胺存在，这表明DMSOR分泌首先在减少和未折叠的形式。在突变体的原生质球中，在非变性凝胶上还检测到一个新的折叠中间体在未折叠和天然形式之间迁移。该中间体不含二硫键，但具有与天然形式相似的折叠紧凑构象。
All of the nine cysteine residues in dimethyl sulfoxide reductase (OMSOR) exist in reduced thiol form. The unfolded form, which was previously detected in DMSOR proteins secreted by spheroplasts prepared from a molybdenum cofactor-deficient mutant, was also detected in spheroplasts from a wild type strain when iodoacetamide was present, suggesting that DMSOR is secreted first in a reduced and unfolded form. In spheroplasts from the mutant, a new folding intermediate migrating between the unfolded and native forms was additionally detected on non-denaturing gel. This intermediate contained no disulfide bonds, but had a folded compact conformation similar to that of the native form.
牛胰蛋白酶抑制剂在大肠杆菌周质中的折叠。
DOI：
--
发表时间：
1994
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Ostermeier,M;Georgiou,G
通讯作者：
Georgiou,G