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Inter-helical hydrogen bonds are essential elements for intra-protein signal transduction: The role of Asp115 in bacteriorhodopsin transport function
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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2007 (English)In: Journal of Molecular Biology, ISSN 0022-2836, E-ISSN 1089-8638, Vol. 368, no 3, 666-676 p.Article in journal (Refereed) Published
Abstract [en]

The behavior of the D115A mutant was analyzed by time-resolved UV-Vis and Fourier transformed infrared (FTIR) spectroscopies, aiming to clarify the role of Asp115 in the intra-protein signal transcluctions occurring during the bacteriorhodopsin photocycle. UV-Vis data on the D115A mutant show severely desynchronized photocycle kinetics. FTIR data show a poor transmission of the retinal isomerization to the chromoprotein, evidenced by strongly attenuated helical changes (amide 1), the remarkable absence of environment alterations and protonation/deprotonation events related to Asp96 and direct Schiff base (SB) protonation form the bulk. This argues for the interactions of Asp115 with Leu87 (via water molecule) and Thr90 as key elements for the effective and vectorial proton path between Asp96 and the SB in the cytoplasmic half of bacteriorhodopsin. The results strongly suggest the presence of a regulation motif enclosed in helices C and D (Thr90-Pro91/Asp115) which drives properly the dynamics of helix C through a set of interactions. It also supports the idea that intra-helical hydrogen bonding clusters in the buried regions of transmembrane proteins can be potential elements in intra-protein signal transduction.

Place, publisher, year, edition, pages
2007. Vol. 368, no 3, 666-676 p.
Keyword [en]
protein dynamics, signal transduction, membrane proteins, time resolved spectroscopies, bacteriorhodopsin
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:su:diva-56597DOI: 10.1016/j.jmb.2007.02.021ISI: 000246060200005OAI: diva2:412981
authorCount :6Available from: 2011-04-27 Created: 2011-04-19 Last updated: 2011-04-27Bibliographically approved

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