July 2008 Volume 15 Number 7, pp 653 - 765
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Nature Methods focus on Single Molecule Analysis - June 2008
Biologists are becoming increasingly interested in methodologies that
can examine the mechanism of action of fundamental biological
processes at the molecular level. This focus will consist of four
review-type articles that provide practical guidance for some of the
techniques that are most integral to in vitro single-molecule
experiments. These will cover single-molecule fluorescence methods,
microfluidic flow cells to manipulate experimental conditions during
experiments, and force spectroscopy techniques such as atomic force
microscopy (AFM) and optical traps to manipulate individual molecules
themselves.
http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0K7N0Ev
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EDITORIAL
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Focus on Membrane Fusion
Bringing it together p653
An in-depth look at membrane fusion-a process essential for
communication within and between cells-is presented in this
issue of Nature Structural & Molecular Biology.
doi:10.1038/nsmb0708-653
http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzET0EA
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ESSAY
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Focus on Membrane Fusion
Some classic papers in the field of membrane fusion-a personal
view pp655 - 657
Every field of research has influential papers that have shaped and
guided future work. Reinhard Jahn gives his picks for membrane fusion
and a little bit of history about how the field has developed.
Reinhard Jahn
doi:10.1038/nsmb0708-655
http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEU0EB
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REVIEWS
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Focus on Membrane Fusion
Membrane fusion pp658 - 664
William Wickner and Randy Schekman
doi:10.1038/nsmb.1451
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEV0EC
Article: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEW0ED
Focus on Membrane Fusion
Synaptic vesicle fusion pp665 - 674
Josep Rizo and Christian Rosenmund
doi:10.1038/nsmb.1450
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEX0EE
Article: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEY0EF
Focus on Membrane Fusion
Mechanics of membrane fusion pp675 - 683
Leonid V Chernomordik and Michael M Kozlov
doi:10.1038/nsmb.1455
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEZ0EG
Article: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEa0EN
Focus on Membrane Fusion
The fusion pores of Ca2+-triggered exocytosis pp684 - 689
Meyer B Jackson and Edwin R Chapman
doi:10.1038/nsmb.1449
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEb0EO
Article: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEc0EP
Focus on Membrane Fusion
Viral membrane fusion pp690 - 698
Stephen C Harrison
doi:10.1038/nsmb.1456
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEd0EQ
Article: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEe0ER
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RESEARCH HIGHLIGHTS
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Research highlights p699
doi:10.1038/nsmb0708-699
http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEf0ES
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ARTICLES
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Supramolecular SNARE assembly precedes hemifusion in SNARE-mediated
membrane fusion pp700 - 706
The cooperative action of multiple trans SNARE complexes are a likely
requirement for successful membrane fusion. New in vitro analyses
reveal the kinetic timescales of the sequential steps of the fusion
process, beginning with trans SNARE pairing and clustering of
vesicle SNARE proteins, proceeding to hemifusion of outer bilayer
leaflets, and ending with full fusion.
Xiaobing Lu, Yinghui Zhang and Yeon-Kyun Shin
doi:10.1038/nsmb.1433
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEg0ET
Article: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEh0EU
Complexin and Ca2+ stimulate SNARE-mediated membrane fusion
pp707 - 713
Complexin is one of several regulatory molecules known to be important
for SNARE-mediated fusion that occurs during neurotransmitter release.
In vitro data now suggest that complexin plays inhibitory and Ca2+-
dependent stimulatory roles that may be correlated to changing
interactions with the SNARE complex.
Tae-Young Yoon et al.
doi:10.1038/nsmb.1446
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEi0EV
Article: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEj0EW
Capped small RNAs and MOV10 in human hepatitis delta virus replication
pp714 - 721
Both genomic and antigenomic hepatitis delta virus (HDV) RNAs have
hairpin-shaped ends. Small capped RNAs have now been identified from
both genomic and antigenomic RNAs, and the human homolog of the
Arabidopsis RNA amplification factor (SDE3) has been implicated in the
replication of HDV.
Dirk Haussecker et al.
doi:10.1038/nsmb.1440
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEk0EX
Article: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEl0EY
Asymmetric bidirectional replication at the human DBF4 origin
pp722 - 729
The origin of replication located at the human DBF4 promoter is finely
characterized. Two initiation zones are on opposite strands and 400 bp
apart, being fired in a sequential way, in a manner similar to
replication at bacterial oriC.
Julia Romero and Hoyun Lee
doi:10.1038/nsmb.1439
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEm0EZ
Article: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEn0Ea
Molecular mechanism of energy conservation in polysulfide respiration
pp730 - 737
Polysulfides are chains of sulfur atoms abundant in extreme
environments. Some organisms reduce polysulfides, and this reaction
may be coupled to respiratory processes. Now the structure of the
multicomponent membrane complex that catalyzes this reaction is
solved, revealing a potential proton channel that could have a role
in energy conservation.
Mika Jormakka et al.
doi:10.1038/nsmb.1434
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEo0Eb
Article: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEp0Ec
Fungal Rtt109 histone acetyltransferase is an unexpected structural
homolog of metazoan p300/CBP pp738 - 745
Rtt109 is a relatively recently identified yeast histone
acetyltransferase that forms distinct complexes with two histone
chaperones. The structure of Rtt109 now reveals that while
functionally distinct, it is structurally homologous to mammalian
p300/CBP, which previously appeared to not contain a counterpart
in yeast.
Yong Tang et al.
doi:10.1038/nsmb.1448
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEq0Ed
Article: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEr0Ee
Mechanism of lid closure in the eukaryotic chaperonin TRiC/CCT
pp746 - 753
Group II chaperonins, such as TriC/CCT, have a build-in lid that can
cover the folding chamber and functions in an analogous way to the
GroES-like proteins used by their Group I counterparts. Structural
and modeling data suggest an allosteric mechanism of TriC lid
closure that differs from GroES-GroEL systems.
Christopher R Booth et al.
doi:10.1038/nsmb.1436
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEs0Ef
Article: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEt0Eg
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TECHNICAL REPORT
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GroEL as a molecular scaffold for structural analysis of the anthrax
toxin pore pp754 - 760
The protective antigen (PA) moiety of anthrax toxin exists as a
stable prepore, converting into the pore form under low pH to
translocate the enzymatic components across the host cell membrane.
The PA pore rapidly aggregates in solution, and it is now shown that
the chaperone GroEL can stabilize the PA pore, allowing
single-particle EM analysis. This method could be useful for other
membrane protein complexes.
Hiroo Katayama et al.
doi:10.1038/nsmb.1442
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEu0Eh
Article: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEv0Ei
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BRIEF COMMUNICATIONS
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A second binding site for double-stranded RNA in TLR3 and
consequences for interferon activation pp761 - 763
Toll-like receptor 3 (TLR3) recognizes double-stranded RNA (dsRNA)
molecules produced by many viruses and activates an inflammatory
response. Synthetic dsRNAs such as small interfering RNAs have been
shown to activate TLR3. Now the TLR3 ectodomain is found to contain
two dsRNA binding sites, and the implications for dsRNA recognition
and selectivity and downstream signaling are discussed.
Nina Pirher et al.
doi:10.1038/nsmb.1453
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEw0Ej
Article: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEx0Ek
Structure of an O-GlcNAc transferase homolog provides insight into
intracellular glycosylation pp764 - 765
Cytoplasmic O-GlcNac modification of proteins is thought to have
dynamic interplay with phosphorylation and thus be involved in
regulation of signaling processes. The complete structure of an
OGT homolog is now presented, suggesting how diverse ligands can
be presented to the active site of the enzyme.
Carlos Martinez-Fleites et al.
doi:10.1038/nsmb.1443
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEy0El
Article: http://ealerts.nature.com/cgi-bin24/DM/y/el5W0Xztnp0Hjh0BzEz0Em
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