RNA Recognition by Transcriptional Antiterminators of the BglG/SacY Family: Mapping of SacY RNA Binding Site

Autor: Michel Kochoyan, Nguyet Le Minh, Vanessa Bloch, Yinshang Yang, Nathalie Declerck, Stéphane Aymerich

Publikováno v: Journal of Molecular Biology. 319:1035-1048

Transcriptional antiterminators of the BglG/SacY family are bacterial regulatory proteins able to prevent the premature arrest of transcription through specific binding to a ribonucleic antiterminator (RAT) sequence. The RNA recognition module of the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::03f584008714cd40ea609b16c86b5fff
https://doi.org/10.1016/s0022-2836(02)00373-x

Hydration and solution structure of nucleic acids

Autor: Michel Kochoyan, Jean Louis Leroy

Publikováno v: Current Opinion in Structural Biology. 5:329-333

Of particular interest among the revelations from recent new DNA structures is the finding that both strands of the repeated DNA sequences found in telomeres and centromeres may adopt alternative conformations. High-definition NMR studies yielded inf

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e79a32a841752dcb2cc7fbec2e671cc5
https://doi.org/10.1016/0959-440x(95)80094-8

Architectural rules of the zinc-finger motif: comparative two-dimensional NMR studies of native and 'aromatic-swap' domains define a 'weakly polar switch'

Autor: Michael A. Weiss, Henry T. Keutmann, Michel Kochoyan

Publikováno v: Proceedings of the National Academy of Sciences. 88:8455-8459

The Zn-finger motif, encoding a globular minidomain with characteristic structure, provides a striking example of a sequence template for protein folding. Insight into architectural rules relating the amino acid sequence of a protein to its structure

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c63860994912a74a2b3521133ec41753
https://doi.org/10.1073/pnas.88.19.8455

Rapid determination of protein solubility and stability conditions for NMR studies using incomplete factorial design

Autor: Michel Kochoyan, Nathalie Declerck, Thierry Gostan, Hélène Déméné, Thierry Ducat

Publikováno v: Journal of Biomolecular NMR
Journal of Biomolecular NMR, Springer Verlag, 2006, 34 (3), pp.137-151. ⟨10.1007/s10858-006-0003-0⟩
Journal of Biomolecular NMR, 2006, 34 (3), pp.137-151. ⟨10.1007/s10858-006-0003-0⟩

International audience; Sample preparation constitutes a crucial and limiting step in structural studies of proteins by NMR. The determination of the solubility and stability (SAS) conditions of biomolecules at millimolar concentrations stays today e

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc25b589a7ec157ec8d6d691942e1889
https://hal.inrae.fr/hal-02668430

The H-NS dimerization domain defines a new fold contributing to DNA recognition

Autor: Vanessa Bloch, Marie Thérèse Augé, Bruno Robert, Stefan T. Arold, Yinshan Yang, Sylvie Rimsky, Emmanuel Margeat, Alain Chavanieu, Michel Kochoyan

Publikováno v: Nature Structural Biology
Nature Structural Biology, Nature Publishing Group, 2003, 10 (3), pp.212-8. 〈10.1038/nsb904〉
Nature Structural Biology, Nature Publishing Group, 2003, 10 (3), pp.212-8. ⟨10.1038/nsb904⟩
Nature Structural Biology, 2003, 10 (3), pp.212-8. ⟨10.1038/nsb904⟩

International audience; H-NS, a protein found in Gram-negative bacteria, is involved in structuring the bacterial chromosome and acts as a global regulator for the expression of a wide variety of genes. These functions are correlated with both its DN

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a979357996c73c86a439136443f31bdf
https://hal.archives-ouvertes.fr/hal-00257410