HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Saveanu, C. Articles by Gilles, A.-M. Search for Related Content PubMed PubMed Citation Articles by Saveanu, C. Articles by Gilles, A.-M. Social Bookmarking                   What's this?

Structural and nucleotide-binding properties of YajQ and YnaF, two Escherichia coli proteins of unknown function

¹ Laboratoire de Chimie Structurale des Macromolécules, (CNRS URA 2185) Institut Pasteur, 75724 Paris Cédex 15, France
² Institut National de la Santé et de la Recherche Médicale U350 and Institut Curie-Recherche, Centre Universitaire, Bâtiments 110-112, 91405 Orsay, France
³ Centre de Biochimie Structurale, Université de Montpellier I, 34000 Montpellier, France
⁴ Unité de Biochimie Structurale (CNRS URA 2185), Institut Pasteur, 75724 Paris Cédex 15, France
⁵ Plateforme Technique Protéomique, Institut Pasteur, 75724 Paris Cédex 15, France

Reprint requests to: Anne-Marie Gilles, Laboratoire de Chimie Structurale des Macromolécules, Institut Pasteur, 28 Rue du Dr Roux, 75724 Paris Cedex 15, France; e-mail: amgilles{at}pasteur.fr; fax: 33 (1) 40 61 39 63.

Structural genomics is a new approach in functional assignment of proteins identified via whole-genome sequencing programs. Its rationale is that nonhomologous proteins performing similar or related biological functions might have similar tertiary structure. We used dye pseudoaffinity chromatography, two-dimensional gel electrophoresis, and mass spectrometry to identify two novel Escherichia coli nucleotide-binding proteins, YnaF and YajQ. YnaF exhibited significant sequence identity with MJ0577, an ATP-binding protein from a hyperthermophile (Methanococcus jannaschii), and with UspA, a protein from Haemophilus influenzae that belongs to the Universal Stress Protein family. YnaF conserves the ATP-binding site and the dimeric structure observed in the crystal of MJ0577. The protein YajQ, present in many bacterial genomes, is missing in eukaryotes. In the absence of significant similarities of YajQ to any solved structure, we determined its structural and ligand-binding properties by NMR and isothermal titration calorimetry. We demonstrate that YajQ is composed of two domains, each centered on a ß-sheet, that are connected by two helical segments. NMR studies, corroborated with local sequence conservation among YajQ homologs in various bacteria, indicate that one of the ß-sheets is mostly involved in biological activity.

Keywords: Structural genomics; YajQ protein; YnaF protein; E. coli; nucleotide binding

CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				X. Qiao, Y. Sun, J. Qiao, and L. Mindich The role of host protein YajQ in the temporal control of transcription in bacteriophage {Phi}6 PNAS, October 14, 2008; 105(41): 15956 - 15960. [Abstract] [Full Text] [PDF]

				C. Archambaud, M.-A. Nahori, J. Pizarro-Cerda, P. Cossart, and O. Dussurget Control of Listeria Superoxide Dismutase by Phosphorylation J. Biol. Chem., October 20, 2006; 281(42): 31812 - 31822. [Abstract] [Full Text] [PDF]

				L. Assairi, T. Bertrand, J. Ferdinand, N. Slavova-Azmanova, M. Christensen, P. Briozzo, F. Schaeffer, C. T. Craescu, J. Neuhard, O. Barzu, et al. Deciphering the function of an ORF: Salmonella enterica DeoM protein is a new mutarotase specific for deoxyribose Protein Sci., May 1, 2004; 13(5): 1295 - 1303. [Abstract] [Full Text] [PDF]