The structure of a PII signaling protein from a halophilic archaeon reveals novel traits and high-salt adaptations

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Title: The structure of a PII signaling protein from a halophilic archaeon reveals novel traits and high-salt adaptations
Authors: Palanca, Carles | Pedro Roig, Laia | Llácer, José Luis | Camacho, Mónica | Bonete, María-José | Rubio, Vicente
Research Group/s: Biotecnología de Extremófilos (BIOTECEXTREM)
Center, Department or Service: Universidad de Alicante. Departamento de Agroquímica y Bioquímica
Keywords: Cell signaling | Crystal structure | GlnK | Haloadaptation | Haloferax mediterranei
Knowledge Area: Bioquímica y Biología Molecular
Issue Date: Aug-2014
Publisher: Wiley
Citation: FEBS Journal. 2014, 281(15): 3299-3314. doi:10.1111/febs.12881
Abstract: To obtain insights into archaeal nitrogen signaling and haloadaptation of the nitrogen/carbon/energy-signaling protein PII, we determined crystal structures of recombinantly produced GlnK2 from the extreme halophilic archaeon Haloferax mediterranei, complexed with AMP or with the PII effectors ADP or ATP, at respective resolutions of 1.49 Å, 1.45 Å, and 2.60 Å. A unique trait of these structures was a three-tongued crown protruding from the trimer body convex side, formed by an 11-residue, N-terminal, highly acidic extension that is absent from structurally studied PII proteins. This extension substantially contributed to the very low pI value, which is a haloadaptive trait of H. mediterranei GlnK2, and participated in hexamer-forming contacts in one crystal. Similar acidic N-extensions are shown here to be common among PII proteins from halophilic organisms. Additional haloadaptive traits prominently represented in H. mediterranei GlnK2 are a very high ratio of small residues to large hydrophobic aliphatic residues, and the highest ratio of polar to nonpolar exposed surface for any structurally characterized PII protein. The presence of a dense hydration layer in the region between the three T-loops might also be a haloadaptation. Other unique findings revealed by the GlnK2 structure that might have functional relevance are: the adoption by its T-loop of a three-turn α-helical conformation, perhaps related to the ability of GlnK2 to directly interact with glutamine synthetase; and the firm binding of AMP, confirmed by biochemical binding studies with ATP, ADP, and AMP, raising the possibility that AMP could be an important PII effector, at least in archaea.
Sponsor: This work was supported by grants from the Spanish government (BFU2011-30407 and BIO2008_00082, to V. Rubio and M. J. Bonete, respectively) and from the Valencian government (Prometeo 2009/51 to V. Rubio). C. Palanca is a JAE-Predoc fellow of the CSIC and, during this work, L. Pedro-Roig was a FPU fellow of the Spanish Ministry of Education. The research leading to these results has received funding from the European Community’s Seventh Framework Programme (FP7/2007–2013) under BioStruct-X (grant agreement No. 283570).
URI: http://hdl.handle.net/10045/44401
ISSN: 1742-464X (Print) | 1742-4658 (Online)
DOI: 10.1111/febs.12881
Language: eng
Type: info:eu-repo/semantics/article
Rights: © 2014 FEBS
Peer Review: si
Publisher version: http://dx.doi.org/10.1111/febs.12881
Appears in Collections:Research funded by the EU
INV - BIOTECEXTREM - Artículos de Revistas

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