Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/47840
Title: Essential residues in the H-NS binding site of Hha, a co-regulator of horizontally acquired genes in Enterobacteria
Author: Fernández de Alba, Carles
Solórzano, Carla
Paytubi Casabona, Sònia
Madrid Xufré, Cristina
Juárez Giménez, Antonio
García, Jesús
Pons Vallès, Miquel
Keywords: Proteïnes
Bacteriologia
ADN
Bioenginyeria
Enterobacteriàcies
Proteins
Bacteriology
DNA
Bioengineering
Enterobacteriaceae
Issue Date: 2011
Publisher: Elsevier B.V.
Abstract: Proteins of the Hha/YmoA family co-regulate with H-NS the expression of horizontally acquired genes in Enterobacteria. Systematic mutations of conserved acidic residues in Hha have allowed the identification of D48 as an essential residue for H-NS binding and the involvement of E25. Mutations of these residues resulted in deregulation of sensitive genes in vivo. D48 is only partially solvent accessible, yet it defines the functional binding interface between Hha and H-NS confirming that Hha has to undergo a conformational change to bind H-NS. Exposed acidic residues, such as E25, may electrostatically facilitate and direct the approach of Hha to the positively charged region of H-NS enabling the formation of the final complex when D48 becomes accessible by a conformational change of Hha.
It is part of: Febs Letters, 2011, vol. 585, num. 12, p. 1765-1770
URI: http://hdl.handle.net/2445/47840
ISSN: 0014-5793
Appears in Collections:Articles publicats en revistes (Química Inorgànica i Orgànica)

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