Localization of the cholesterol oxidase in Rhodococcus erythropolis IMET 7185 studied by immunoelectron microscopy

Atrat, P.; Wagner, Barbara; Wagner, Manfred; Schumann, Gerald von

doi:10.1016/0960-0760(92)90028-h

Cited by 21 publications

(7 citation statements)

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“…The results obtained are coherent with those presented in a previous study in shaken flasks [9], where extracellular COX production is large and arises from the partial solubilization of the cell-linked enzyme [20,21]. After 70 hours of fermentation the total enzyme activity obtained was ca.…”

Section: Resultssupporting

confidence: 90%

Rhodococcus erythropolis ATCC 25544 as a suitable source of cholesterol oxidase: cell-linked and extracellular enzyme synthesis, purification and concentration

2002

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Section: Resultssupporting

confidence: 90%

Rhodococcus erythropolis ATCC 25544 as a suitable source of cholesterol oxidase: cell-linked and extracellular enzyme synthesis, purification and concentration

2002

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“…[4][5][6][7][8]. The strains able to overproduction of ChO were obtained by genetic engineering [9].…”

Section: Introductionmentioning

confidence: 99%

Extracellular 3β-hydroxysteroid oxidase of Mycobacterium vaccae VKM Ac-1815D

Nikolayeva

Egorova

Dovbnya

et al. 2004

The Journal of Steroid Biochemistry and Molecular Biology

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“…The cell wall of certain rhodococci contains up to 10% protein by weight (8). However, with a few exceptions (1), the function of the cell wall proteins is not known so far. It has been predicted, however (38), that rhodococci must contain cell wall porins similar to those of other members of the group of mycolic-acid containing actinomycetes, such as nocardia (33,34), mycobacteria (39,40,41), and corynebacteria (19).…”

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confidence: 99%

Biochemical Identification and Biophysical Characterization of a Channel-Forming Protein from Rhodococcus erythropolis

2000

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Organic solvent extracts of whole cells of the gram-positive bacterium Rhodococcus erythropolis contain a channel-forming protein. It was identified by lipid bilayer experiments and purified to homogeneity by preparative sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE). The pure protein had a rather low molecular mass of about 8.4 kDa, as judged by SDS-PAGE. SDS-resistant oligomers with a molecular mass of 67 kDa were also observed, suggesting that the channel is formed by a protein oligomer. The monomer was subjected to partial protein sequencing, and 45 amino acids were resolved. According to the partial sequence, the sequence has no significant homology to known protein sequences. To check whether the channel was indeed localized in the cell wall, the cell wall fraction was separated from the cytoplasmic membrane by sucrose step gradient centrifugation. The highest channel-forming activity was found in the cell wall fraction. The purified protein formed large ion-permeable channels in lipid bilayer membranes with a single-channel conductance of 6.0 nS in 1 M KCl. Zero-current membrane potential measurements with different salts suggested that the channel of R. erythropolis was highly cation selective because of negative charges localized at the channel mouth. The correction of single-channel conductance data for negatively charged point charges and the Renkin correction factor suggested that the diameter of the cell wall channel is about 2.0 nm. The channel-forming properties of the cell wall channel of R. erythropolis were compared with those of other members of the mycolata. These channels have common features because they form large, water-filled channels that contain net point charges.

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Localization of the cholesterol oxidase in Rhodococcus erythropolis IMET 7185 studied by immunoelectron microscopy

Cited by 21 publications

References 21 publications

Rhodococcus erythropolis ATCC 25544 as a suitable source of cholesterol oxidase: cell-linked and extracellular enzyme synthesis, purification and concentration

Rhodococcus erythropolis ATCC 25544 as a suitable source of cholesterol oxidase: cell-linked and extracellular enzyme synthesis, purification and concentration

Extracellular 3β-hydroxysteroid oxidase of Mycobacterium vaccae VKM Ac-1815D

Biochemical Identification and Biophysical Characterization of a Channel-Forming Protein from Rhodococcus erythropolis

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