La sculpture funéraire à Marseille aux IVe et Ve siècles

Drocourt, Daniel; Drocourt, Geneviève

doi:10.3406/bulmo.1974.5314

Cited by 2 publications

(2 citation statements)

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“…The binding of transglycosylase to blue Sepharose and poly(U)-Sepharose and the concomitant interaction with polynucleotides is not a unique feature of only this enzyme: another murein hydrolase from E. coli, a murein endopeptidase [16a], interferon from mouse [17] and the polynucleotide phosphorylase from E. coli [18] all show these properties.…”

Section: Inhibition Of Transglycosylase Activity By Polyanionic Polymmentioning

confidence: 99%

Escherichia coli Murein Transglycosylase

Kusser

Schwarz

1980

European Journal of Biochemistry

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Escherichia coli murein transglycosylase, a potential autolysin which splits the sugar chains of the murein sacculus, was rapidly purified from a crude cell extract by sequential chromatography on columns of blue Sepharose and poly(U)‐Sepharose. In accordance with the binding to blue Sepharose and poly(U)‐Sepharose, the transglycosylase is inhibited by Cibacron blue F3G‐A, the affinity ligand of blue Sepharose, and also by polynucleotides, the latter, however, with varying efficiency. Among the polynucleotides tested, single‐stranded DNA was found to be one of the most potent inhibitors. When bound to a blue Sepharose column, transglycosylase could be displaced from the column with single‐stranded DNA. Taken together, these results point to a polynucleotide binding area on the transglycosylase molecule. Some aspects of the blue Sepharose affinity chromatography and the possible biological significance of the transglycosylase are discussed.

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Section: Inhibition Of Transglycosylase Activity By Polyanionic Polymmentioning

confidence: 99%

Escherichia coli Murein Transglycosylase

Kusser

Schwarz

1980

European Journal of Biochemistry

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“…The three families of structures should also be analyzed in the broad context of antibiotic resistance for Bm analogues such as phleomycin and tallysomycin (14). It has been reported that these molecules can also bind to BLMT and ShBle (12,51) and thus carry antibiotic resistance. Their chemical structures are reported in Supporting Information Figure 3.…”

Section: Discussionmentioning

confidence: 99%

NMR Study of the Interaction between Zn(II) Ligated Bleomycin and Streptoalloteichus hindustanus Bleomycin Resistance Protein

et al. 2003

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Bleomycin (Bm), a 1.4 kDa glycopeptide excreted by Streptomyces verticillus, is a natural antibacterial compound used in therapy as antineoplastic drug. To counteract its biological activity, cells have developed several resistance mechanisms, one of these based on proteins able to tightly bind Bm. In this paper, the interaction of Zn(2+)-Bm with the Streptoalloteichus hindustanus Bm resistance protein (ShBle) has been investigated by solution state NMR. Sequential nOe and chemical shift index have shown that the fold of the protein (in absence or presence of Bm) is identical to the previously published X-ray structure. The dimeric nature of ShBle is confirmed by the diffusion tensor as determined by NMR relaxation data. Using isotope filtered nOe experiment, intermolecular nOes between Bm and ShBle have been observed as used for modeling. While the interaction of the Bm metal binding site with ShBle appears to be uniquely defined, several conformations of the bithiazole moieties are compatible with the NMR data. Binding of Bm also induces changes of the local dynamics (stretch N85-G91), as shown by (15)N relaxation data. These results are discussed in the context of several Bm analogues able to interact with ShBle and of the recently published X-rays structures.

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La sculpture funéraire à Marseille aux IVe et Ve siècles

Cited by 2 publications

References 1 publication

Escherichia coli Murein Transglycosylase

Escherichia coli Murein Transglycosylase

NMR Study of the Interaction between Zn(II) Ligated Bleomycin and Streptoalloteichus hindustanus Bleomycin Resistance Protein

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