Nanotubes connecting B, subtilis and S. aureusFIGURE 6, CELL 44:590 - 600, 2011
1. Nanoscale bacterial swapUsing high-resolution electron microscopy, researchers discovered nanotube-like structures in bacteria that enable them to exchange cytosolic material, even between different species. At around 1 µm wide, the tubes represent an entirely new mechanism of bacterial exchange.
G. P. Dubey and S. Ben-Yehuda, "Intercellular Nanotubes Mediate Bacterial Communication," Cell, 144:590-600, 2011. DOI: 10.1016/j.cell.2011.01.015
2. TRIMming HIVThe TRIM5 protein, which promotes the disassembly of the HIV viral capsid, has been known to make certain monkey species, such as rhesus macaques, resistant to HIV. Now, by interrogating TRIM5’s interaction with over 20 immune signaling proteins, researchers find that it acts as a pattern-recognition receptor as well as mediates the activation of proinflammatory pathways.
T. Pertel, et. al., "TRIM5 is an innate immune sensor for the retrovirus capsid lattice," Nature, 472:361-5, 2011.
G. Xy, et. al., "Crystal structure of inhibitor of kappaB kinase beta," Nature, 472, 325–330, 2011.
4. Enzymatic self-controlA crystal structure of an E. coli ATPase, an enzyme which catalyzes the energetic breakdown of ATP into ADP, reveals a surprising self-inhibitory state in which one of its eight subunits is extended, thus preventing the rotation of another subunit necessary for ATP hydrolysis.
G. Cingolani and T.M. Duncan, "Structure of the ATP synthase catalytic complex (F(1)) from Escherichia coli in an autoinhibited conformation," Nat Struct Mol Biol, 18:701-7, 2011.
5. The making of piliIn yet another groundbreaking crystal structure, a bacterial membrane protein, FimD, is visualized as it transports a pilus unit along with its chaperon across the bacterial membrane. The finding promises to enhance the current understanding of pilus assembly.
G. Phan, et. al., "Crystal structure of the FimD usher bound to its cognate FimC-FimH substrate," Nature, 474:49-53, 2011.
6. Disorder fights disorderResearchers found that one of the cell’s crucial quality control proteins, which detects and degrades misfolded proteins, is itself an intrinsically disordered protein—a property that allows the protein to recognize a wide variety of substrates.
J.C. Rosenbaum, et. al., "Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates," Mol Cell. 41:93-106, 2011.
7. The twitching riboswitchRiboswitches are cellular sensors that turn genes on or off in response to the presence of other cellular factors, such as metabolic products. Researchers working on the riboswitch known as S-adenosylmethionine (SAM) II found that it’s able to carry out its functions only by undergoing major structural changes, which the authors described as “twitching.”
A. Haller, et. al., "Conformational capture of the SAM-II riboswitch," Nature Chemical Biology, 7:393–400, 2011.
The F1000 Top 7 is a snapshot of the highest ranked articles from a 30-day period on Faculty of 1000 in biochemistry and related areas, as calculated on June 23, 2011. Faculty Members evaluate and rate the most important papers in their field. To see the latest rankings, search the database, and read daily evaluations, visit http://f1000.com.
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