Scott Classen: March 2012 Archives

Researchers from Scripps Research Institute and the University of Glasgow have published a detailed molecular model of how UVR8, a unique heme-free plant photoreceptor, senses UV-B light via an intricate interacting mesh of Tryptophan residues positioned at the UVR8 dimer interface which ultimately results in the disruption of a salt bridge and dissociation of the UVR8 dimer.

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The recently identified plant photoreceptor UVR8 triggers regulatory changes in gene expression in response to ultraviolet-B (UV-B) light via an unknown mechanism. Here, crystallographic and solution structures of the UVR8 homodimer, together with mutagenesis and far-UV circular dichroism spectroscopy, reveal its mechanisms for UV-B perception and signal transduction. β-propeller subunits form a remarkable, tryptophan-dominated, dimer interface stitched together by a complex salt-bridge network. Salt-bridging arginines flank the excitonically coupled cross-dimer tryptophan “pyramid” responsible for UV-B sensing. Photoreception reversibly disrupts salt bridges, triggering dimer dissociation and signal initiation. Mutation of a single tryptophan to phenylalanine retunes the photoreceptor to detect UV-C wavelengths. Our analyses establish how UVR8 functions as a photoreceptor without a prosthetic chromophore to promote plant development and survival in sunlight.

Christie, J. M., Arvai, A. S., Baxter, K. J., Heilmann, M., Pratt, A. J., O’Hara, A., Kelly, S. M., Hothorn, M., Smith, B. O., Hitomi, K., Jenkins, G. I., Getzoff, D. G.”Plant UVR8 Photoreceptor Senses UV-B by Tryptophan-Mediated Disruption of Cross-Dimer Salt Bridges” Science. Published Online February 9 2012

Members of the Noller lab recently published a 3.3 Å resolution structure of a complex containing the ribosomal release factor (RF3) locked in its GTP-bound state (mimicked using GDPNP) in association with the E. coli 70s ribosome. Crystallographic data for this project was collected at the SIBYLS beamline MX station.

The class II release factor RF3 is a GTPase related to elongation factor EF-G, which catalyzes release of class I release factors RF1 and RF2 from the ribosome after termination of protein synthesis. The 3.3 Å crystal structure of the RF3·GDPNP·ribosome complex provides a high-resolution description of interactions and structural rearrangements that occur when binding of this translational GTPase induces large-scale rotational movements in the ribosome. RF3 induces a 7° rotation of the body and 14° rotation of the head of the 30S ribosomal subunit, and itself undergoes inter- and intradomain conformational rearrangements. We suggest that ordering of critical elements of switch loop I and the P loop, which help to form the GTPase catalytic site, are caused by interactions between the G domain of RF3 and the sarcin-ricin loop of 23S rRNA. The rotational movements in the ribosome induced by RF3, and its distinctly different binding orientation to the sarcin-ricin loop of 23S rRNA, raise interesting implications for the mechanism of action of EF-G in translocation.


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Zhou, J., Lancaster, L., Trakhanov, S., & Noller, H. F. “Crystal structure of release factor RF3 trapped in the GTP state on a rotated conformation of the ribosome.” RNA (New York, NY), 18(2), 230-240.

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