Detection of a Compact Folding Intermediate of Dimethyl Sulfoxide Reductase Secreted from a Molybdenum Cofactor-Deficient Mutant ofRhodobacter sphaeroidesf. sp. denitrificans

Autor:	Masahiro Matsuzaki, Toshio Satoh
Rok vydání:	1997
Předmět:	biology Physiology fungi Mutant Cell Biology Plant Science General Medicine Spheroplast biology.organism_classification chemistry.chemical_compound Rhodobacter sphaeroides chemistry Biochemistry Iodoacetamide Protein folding Molybdenum cofactor Rhodospirillaceae Cysteine
Zdroj:	Plant and Cell Physiology. 38:1286-1290
ISSN:	1471-9053 0032-0781
DOI:	10.1093/oxfordjournals.pcp.a029118
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::ef7a799d6312b33d07c1ad78d928d21c https://doi.org/10.1093/oxfordjournals.pcp.a029118 Zobrazit plný text záznamu Plný text ve formátu PDF