March 2010 Volume 17 Number 3, pp 259 - 388
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EDITORIAL
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In times of crisis p259
doi:10.1038/nsmb0310-259
In some countries, science funding has seen a cash boost intended to
stimulate long-term research efforts and competitiveness in response
to the global economic crisis; in others, researchers and university
employees are being forced to tighten their belts to accommodate
budget deficits.
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NEWS AND VIEWS
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Synaptotagmin-SNARE coupling enlightened pp260 - 262
Josep Rizo
doi:10.1038/nsmb0310-260
Synaptotagmins and SNAREs are known to couple Ca2+ sensing to
membrane fusion during Ca2+-triggered exocytosis, but unraveling
the mechanism of this coupling has proven extremely difficult.
Two studies in this issue now provide crucial insights into the
nature of synaptotagmin-SNARE interactions and reveal unsuspected
similarities between synaptotagmins and viral fusion proteins.
http://links.ealert.nature.com/ctt?kn=10&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
Channeling sperm activation p262
Sabbi Lall
doi:10.1038/nsmb0310-262
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RESEARCH HIGHLIGHTS
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Research highlights p263
doi:10.1038/nsmb0310-263
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ARTICLES
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Intersubunit capture of regulatory segments is a component of
cooperative CaMKII activation pp264 - 272
Luke H Chao et al.
doi:10.1038/nsmb.1751
The CaMKII complex can enter a state of Ca2+-independent activity
in response to high frequency Ca2+ pulses. Using functional and
structural analyses, it is now shown that activation is cooperative
and the basis of this is the intersubunit capture of the regulatory
subunit of one kinase module by its neighbor.
Abstract: http://links.ealert.nature.com/ctt?kn=28&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=114&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
Mediator Head module structure and functional interactions
pp273 - 279
Gang Cai et al.
doi:10.1038/nsmb.1757
By controlling interaction with RNA polymerase II, the Head module
portion of Mediator plays a critical role in transcriptional
regulation. A study now characterizes different conformations of
the Head and also its interaction with polymerase and the
TATA-binding protein.
Abstract: http://links.ealert.nature.com/ctt?kn=30&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=107&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
Munc13 C2B domain is an activity-dependent Ca2+ regulator of synaptic
exocytosis pp280 - 288
Ok-Ho Shin et al.
doi:10.1038/nsmb.1758
Munc13 primes synaptic vesicles for exocytosis. Studies now reveal
that the central C2B domain of Munc13 contains a structurally unusual
Ca2+ binding site that confers specific phospholipid-binding
properties to Munc13 and is essential for regulating exocytosis upon
trains of action potentials.
Abstract: http://links.ealert.nature.com/ctt?kn=33&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=93&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
The structures of the anti-tuberculosis antibiotics viomycin and
capreomycin bound to the 70S ribosome pp289 - 293
Robin E Stanley et al.
doi:10.1038/nsmb.1755
The tuberactinomycin antibiotic family is one of the most effective
against multi-drug resistant M. tuberculosis. The structures of two
members of this family, viomycin and capreomycin, bound to the
ribosome now indicate that they act by stabilizing the A site tRNA
in a pre-translocation state and may suggest further avenues for
drug development.
Abstract: http://links.ealert.nature.com/ctt?kn=35&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=91&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
The structure of the catalytic subunit FANCL of the Fanconi anemia
core complex pp294 - 298
Ambrose R Cole, Laurence P C Lewis and Helen Walden
doi:10.1038/nsmb.1759
The crystal structure of FANCL, the catalytic subunit of the Fanconi
Anemia core complex, reveals an unexpected domain architecture. The
molecule comprises an N-terminal E2-like fold, a novel double-RWD
domain, which is found to be responsible for substrate binding,
and a C-terminal RING domain that is predicted to facilitate E2
binding.
Abstract: http://links.ealert.nature.com/ctt?kn=37&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=86&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
Systematic identification of fragile sites via genome-wide location
analysis of gamma-H2AX pp299 - 305
Rachel K Szilard et al.
doi:10.1038/nsmb.1754
H2AX phosphorylation is an early response to DNA damage and is
mediated by the ATM/ATR kinases. By examining the genome-wide
location of gamma-H2A in wild type and mutant S. cerevisiae
strains, loci that tend to engage ATR (Mec1) and ATM (Tel1) are
identified as a route to mapping fragile sites in this genome.
Abstract: http://links.ealert.nature.com/ctt?kn=39&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=85&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
SF2/ASF autoregulation involves multiple layers of post-transcriptional
and translational control pp306 - 312
Shuying Sun et al.
doi:10.1038/nsmb.1750
SF2/ASF is a key splicing factor and is abnormally overexpressed
in some tumors. By examining the post-transcriptional regulation
of this factor, it is now found that SF2/ASF downregulates its own
expression through multiple mechanisms.
Abstract: http://links.ealert.nature.com/ctt?kn=41&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=63&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
alpha-Helical nascent polypeptide chains visualized within distinct
regions of the ribosomal exit tunnel pp313 - 317
Shashi Bhushan et al.
doi:10.1038/nsmb.1756
Previous studies argued that nascent polypeptide chains can form
secondary structure in the ribosome exit tunnel despite spatial
constraints. Using single-particle cryo-EM reconstructions of
eukaryotic ribosomes carrying nascent chains with high helical
propensity, density consistent with helix formation is now observed
in the exit tunnel as are interactions with tunnel proteins.
Abstract: http://links.ealert.nature.com/ctt?kn=43&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=69&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
Single-molecule FRET-derived model of the synaptotagmin 1-SNARE
fusion complex pp318 - 324
Ucheor B Choi et al.
doi:10.1038/nsmb.1763
Single-molecule FRET studies have resulted in an experimentally
derived model of a synaptotagmin-SNARE complex. In this complex of
SNARE with synaptotagmin 1, the arrangement of the Ca2+-binding
loops is similar to that of the structure of SNARE-induced Ca2+-bound
synaptotagmin 3. This suggests a common molecular mechanism by which
the synaptotagmin-SNARE interaction plays a role in Ca2+-triggered
vesicle fusion.
Abstract: http://links.ealert.nature.com/ctt?kn=45&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=12&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
Molecular mechanism of the synaptotagmin-SNARE interaction in
Ca2+-triggered vesicle fusion pp325 - 331
Marija Vrljic et al.
doi:10.1038/nsmb.1764
The interaction between synaptotagmin and SNAREs was characterized
by a combination of single-molecule FRET and crystallography. The
arrangement of the two Ca2+-binding loops of synaptotagmin 3 within
SNARE-induced Ca2+-bound synaptotagmin 3 matches that of SNARE-bound
synaptotagmin 1, suggesting a common molecular mechanism by which the
synaptotagmin-SNARE interaction plays a role in Ca2+-triggered vesicle
fusion.
Abstract: http://links.ealert.nature.com/ctt?kn=47&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=13&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
A distinct mechanism for the ABC transporter BtuCD-BtuF revealed by
the dynamics of complex formation pp332 - 338
Oded Lewinson, Allen T Lee, Kaspar P Locher and Douglas C Rees
doi:10.1038/nsmb.1770
ABC transporters move substrates across the membrane. The substrate
is often delivered by a binding protein. Functional analysis of the
bacterial BtuCD-F system now reveals a distinct mechanism for
substrate delivery different from other ABC transporters, whereby
the binding protein associates with the transporter in the absence
of substrate, and substrate or ATP binding destabilize the complex.
Abstract: http://links.ealert.nature.com/ctt?kn=104&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=29&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
T-cadherin structures reveal a novel adhesive binding mechanism
pp339 - 347
Carlo Ciatto et al.
doi:10.1038/nsmb.1781
T-cadherin is a non-classical GPI-anchored cadherin. The crystal
structures of T-cadherins from different organisms now reveal that
the EC1-EC2 regions can form dimers via an interface near the EC1-EC2
calcium binding sites, different from the EC1 strand swapping seen in
classical cadherin homophilic interactions.
Abstract: http://links.ealert.nature.com/ctt?kn=101&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=44&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
Two-step adhesive binding by classical cadherins pp348 - 357
Oliver J Harrison et al.
doi:10.1038/nsmb.1784
Classical cadherins form two types of dimers: a strand swap version
and an "X dimer" that lacks strand exchange between monomers. Strand
swapping mutants are now found to form the X-dimer structure. Together
with further experiments, this supports the idea that the X-dimer is
an intermediate configuration that promotes strand swapped dimer
formation.
Abstract: http://links.ealert.nature.com/ctt?kn=103&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=50&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
One SNARE complex is sufficient for membrane fusion pp358 - 364
Geert van den Bogaart et al.
doi:10.1038/nsmb.1748
Most intracellular membrane fusion reactions in eukaryotes are
mediated by SNARE proteins present in both fusing membranes. It
has been unclear how many SNARE complexes are needed for fusion.
FRET studies now show that liposomes with a single SNARE molecule
are able to fuse with other liposomes or with purified synaptic
vesicles.
Abstract: http://links.ealert.nature.com/ctt?kn=99&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=48&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA
repair via homologous recombination pp365 - 372
Dong-Hyun Lee et al.
doi:10.1038/nsmb.1769
Upon formation of DNA double-strand breaks, many protein
phosphorylation events are involved in activating cellular
responses and DNA repair processes. Now a phosphatase complex
containing PP4C and regulatory subunit PP4R2 is shown to
dephosphorylate RPA2, and this is necessary to allow efficient
DNA repair via homologous recombination.
Abstract: http://links.ealert.nature.com/ctt?kn=100&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=62&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
The structure of the peripheral stalk of Thermus thermophilus
H+-ATPase/synthase pp373 - 378
Lawrence K Lee et al.
doi:10.1038/nsmb.1761
The crystal structure of the peripheral stalk of the A-type
ATPase/synthase (A-ATPase) from Thermus thermophilus reveals a
heterodimeric right-handed coiled coil, a protein fold never
observed before. Fitting of the stalk structure into the EM density
of intact A-ATPase provides the most complete composite model so far.
Abstract: http://links.ealert.nature.com/ctt?kn=111&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=66&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
Mechanism of error-free and semitargeted mutagenic bypass of an
aromatic amine lesion by Y-family polymerase Dpo4 pp379 - 388
Olga Rechkoblit et al.
doi:10.1038/nsmb.1771
Aromatic amines can form covalent DNA adducts, in which the damaged
base can cause mutations in the vicinity of the lesion. A mechanism
for such semi-targeted mutagenesis is now proposed, based on
structural and functional data on Dpo4: the bulky lesion-bypass
polymerase interaction leads to a conformation of Dpo4 that stabilizes
misaligned intermediates.
Abstract: http://links.ealert.nature.com/ctt?kn=113&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=79&m=34677370&r=MTc2OTcxOTY5MQS2&b=2&j=NjgzMzA2MTYS1&mt=1&rt=0
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