Identification of coevolving residues and coevolution potentials emphasizing structure, bond formation and catalytic coordination in protein evolution.

Autor: Daniel Y Little, Lu Chen

Publikováno v: PLoS ONE, Vol 4, Iss 3, p e4762 (2009)

The structure and function of a protein is dependent on coordinated interactions between its residues. The selective pressures associated with a mutation at one site should therefore depend on the amino acid identity of interacting sites. Mutual info

Externí odkaz: https://doaj.org/article/5246f8f415054d408bd275b0e390f051

The putative high-affinity nitrate transporter NRT2.1 represses lateral root initiation in response to nutritional cues

Autor: Jocelyn E. Malamy, Sabrina Oliva, Anne Krapp, Hongyu Rao, Françoise Daniel-Vedele, Daniel Y. Little

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America 38 (102), 13693-13698. (2005)
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2005, 102 (38), pp.13693-13698. ⟨10.1073/pnas.0504219102⟩

Lateral root initiation is strongly repressed in Arabidopsis by the combination of high external sucrose and low external nitrate. A previously isolated mutant, lin1 , can overcome this repression. Here, we show that lin1 carries a missense mutation

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07942e8be1c6558a3309645ccd39ff4c
http://prodinra.inra.fr/record/13163