May 2009 Volume 16 Number 5, pp 453 - 572
Visit Nature Structural & Molecular Biology online to browse the
journal.
Now available at http://links.ealert.nature.com/ctt?kn=34&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
Please note that you need to be a subscriber to enjoy full text
access to Nature Structural & Molecular Biology online. To purchase
a subscription, please visit:
http://links.ealert.nature.com/ctt?kn=118&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
Alternatively, to recommend a subscription to your library, please
visit
http://links.ealert.nature.com/ctt?kn=42&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
=========================== ADVERTISEMENT ===========================
Tune Up Your Protein Expression�Join the Fast Lane with DNA2.0's
Codon Optimized Genes and pJexpress Vectors.
Achieve protein expression yields that wt genes and traditional pET
vectors can't match. Codon optimized genes overcome inherent
expression barriers. Combine a DNA2.0 optimized gene with a pJexpress
vector and put your research into the express lane. See the data.
http://links.ealert.nature.com/ctt?kn=69&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
=====================================================================
=========================== ADVERTISEMENT ===========================
Protein modifications: beyond the usual suspects
EMBO reports web focus
Get a sense of the molecular diversity that exists within cells! This series of comprehensive and engaging reviews highlights the complexity of post-translational protein modifications. Leading experts analyze atypical ubiquitin-chain formation, ATGylation, polyglutamylation, neddylation, and Urmylation, and update our knowledge on poly(ADP-ribosyl)ation and O-GlcNAcylation. A complex but important topic to understand!
http://links.ealert.nature.com/ctt?kn=17&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
=====================================================================
----------------------
EDITORIAL
----------------------
Locavore science p453
As we set off into the full swing of traveling for the globally
oriented meeting season, it's worth also remembering the delights of
local science consumption.
doi:10.1038/nsmb0509-453
http://links.ealert.nature.com/ctt?kn=8&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
----------------------
CORRESPONDENCE
----------------------
Mechanisms of APOBEC3G-catalyzed processive deamination of
deoxycytidine on single-stranded DNA pp454 - 455
Linda Chelico, Phuong Pham and Myron F Goodman
doi:10.1038/nsmb0509-454
http://links.ealert.nature.com/ctt?kn=101&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
Reply to "Mechanisms of APOBEC3G-catalyzed processive
deamination of deoxycytidine on single-stranded DNA"
pp455 - 456
Roni Nowarski, Elena Britan-Rosich and Moshe Kotler
doi:10.1038/nsmb0509-455
http://links.ealert.nature.com/ctt?kn=46&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
----------------------
NEWS AND VIEWS
----------------------
Nuclear transport comes full circle pp457 - 459
Previous structural snapshots of snurportin have provided insights
into its cargo recognition and nuclear import. The structure of
snurportin bound to its export factor CRM1 now reveals the molecular
basis of its recycling back into the cytoplasm, illuminating general
principles of nuclear export sequence recognition.
Erik W Debler, Gunter Blobel and Andre Hoelz
doi:10.1038/nsmb0509-457
http://links.ealert.nature.com/ctt?kn=73&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
Going round in circles: the structural biology of type III secretion
systems pp459 - 460
Type III secretions systems (T3SSs) are major bacterial virulence
factors responsible for secretion and injection of protein effectors
into host cells. New structures illuminate their ring structure and
identify novel ring-mediating structural scaffolds.
Gabriel Waksman
doi:10.1038/nsmb0509-459
http://links.ealert.nature.com/ctt?kn=60&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
----------------------
RESEARCH HIGHLIGHTS
----------------------
Research highlights p461
doi:10.1038/nsmb0509-461
http://links.ealert.nature.com/ctt?kn=41&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
----------------------
PERSPECTIVE
----------------------
Metabolism control by the circadian clock and vice versa
pp462 - 467
Kristin Eckel-Mahan and Paolo Sassone-Corsi
doi:10.1038/nsmb.1595
Abstract: http://links.ealert.nature.com/ctt?kn=97&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=74&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
----------------------
ARTICLES
----------------------
A conserved structural motif mediates formation of the periplasmic
rings in the type III secretion system pp468 - 476
The type III secretion system (T3SS) of pathogenic bacteria is
composed of a series of rings in the inner and outer bacterial
membranes. Crystallographic studies of EscJ and PrgH, proteins
that comprise the two inner membrane rings of the T3SS, suggest
that a conserved structural motif serves as a platform for ring
assembly. Additional docking and modeling studies reveal details
of the T3SS architecture and assembly.
Thomas Spreter et al.
doi:10.1038/nsmb.1603
Abstract: http://links.ealert.nature.com/ctt?kn=92&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=96&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
Three-dimensional reconstruction of the Shigella T3SS transmembrane
regions reveals 12-fold symmetry and novel features throughout
pp477 - 485
Gram-negative bacteria use type III secretion systems (T3SSs) to
pass virulence factors into host cells, making them potential
therapeutic targets to combat bacterial infection. A new EM
study of the needle complex from the Shigella T3SS reveals
12-fold symmetry throughout and suggests interactions important
for self-assembly and complex stability.
Julie L Hodgkinson et al.
doi:10.1038/nsmb.1599
Abstract: http://links.ealert.nature.com/ctt?kn=9&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=88&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
Gemin5-snRNA interaction reveals an RNA binding function for WD
repeat domains pp486 - 491
Gemin5 is a WD repeat protein that binds small nuclear RNAs (snRNAs)
through a specific sequence in the context of the SMN complex, a
function required for spliceosomal snRNP biogenesis. Reduced levels
of SMN cause spinal muscular atrophy. A series of biochemical
experiments now indicate that the WD repeat region of Gemin5
recognizes the snRNAs in a sequence-specific fashion, suggesting
that WD repeats are capable of RNA binding.
Chi-kong Lau, Jennifer L Bachorik and Gideon Dreyfuss
doi:10.1038/nsmb.1584
Abstract: http://links.ealert.nature.com/ctt?kn=23&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=128&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
miR-24-mediated downregulation of H2AX suppresses DNA repair in
terminally differentiated blood cells pp492 - 498
Most terminally differentiated cells have a diminished capacity to
respond to and repair DNA damage. Now a microRNA is shown to have a
role in this phenotype in blood cells: miR-24 is upregulated in
blood cells differentiated in vitro and decreases the levels of
H2AX, a histone variant with a key role in the response to DNA
double-stranded breaks.
Ashish Lal et al.
doi:10.1038/nsmb.1589
Abstract: http://links.ealert.nature.com/ctt?kn=102&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=77&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
Structure of the RAG1 nonamer binding domain with DNA reveals a
dimer that mediates DNA synapsis pp499 - 508
V(D)J recombination is mediated by the products of the recombination
activation genes, RAG1 and RAG2. DNA binding and cleavage are
targeted by recombination sequences that flank each gene segment and
are composed of well-conserved heptamer and nonamer sequences
separated either by 12 or 23 base pairs. Schatz and co-workers
report the crystal structure of the RAG1 nonamer binding domain
(NBD) bound to its cognate sequence. The NBD adopts an intertwined
dimer that mediates the synapsis of two DNA molecules. Biochemical
and FRET experiments support the structural findings and have
implications for the regulation of DNA binding and cleavage by RAG1/2.
Fang Fang Yin et al.
doi:10.1038/nsmb.1593
Abstract: http://links.ealert.nature.com/ctt?kn=15&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=26&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
Molecular mimicry of SUMO promotes DNA repair pp509 - 516
Dysfunction of SUMO or Rad60 causes overlapping phenotypes that
include genomic instability. Now, a nonsubstrate interaction between
SUMO-like domain 2 (SLD2) of Rad60 and the SUMO-conjugating enzyme
Ubc9 is shown to suppress aberrant replication-associated homologous
recombination. Thus, SUMO mimicry provides critical regulation in the
SUMO pathway.
John Prudden et al.
doi:10.1038/nsmb.1582
Abstract: http://links.ealert.nature.com/ctt?kn=1&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=64&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
Active nuclear import and cytoplasmic retention of activation-induced
deaminase pp517 - 527
The enzyme activation-induced deaminase (AID) promotes antibody
diversification after B-cell activation, by causing mutagenic lesions
on DNA. Hence, AID's actions must be tightly controlled. AID is found
mainly in the cytosolic compartment and contains a known nuclear
export sequence. Now a structural nuclear localization sequence and
a cytosolic-retention determinant are identified in AID and found to
have a role in localization and function.
Anne-Marie Patenaude et al.
doi:10.1038/nsmb.1598
Abstract: http://links.ealert.nature.com/ctt?kn=25&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=115&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
Insights into substrate stabilization from snapshots of the peptidyl
transferase center of the intact 70S ribosome pp528 - 533
Protein synthesis is catalyzed in the peptidyl transferase center of
the ribosome. The structure of the 70S ribosome containing tRNAs now
gives insight into the active site of a complete ribosome and reveals
a direct interaction between the tRNA substrate and ribosomal proteins.
Rebecca M Voorhees et al.
doi:10.1038/nsmb.1577
Abstract: http://links.ealert.nature.com/ctt?kn=123&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=3&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
Single-molecule force spectroscopy reveals a highly compliant helical
folding for the 30-nm chromatin fiber pp534 - 540
In eukaryotic cells, DNA is wrapped around histones to form
nucleosomes, which are further organized into the 30-nm chromatin
fiber. A single-molecule study with homogeneous chromatin fibers now
shows that the chromatin fiber behaves as a simple spring,
stretching up to three times in response to pulling, a behavior
indicative of a one-start helix structure. Linker histones stabilize
the fiber but do not make it stiffer.
Maarten Kruithof et al.
doi:10.1038/nsmb.1590
Abstract: http://links.ealert.nature.com/ctt?kn=121&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=62&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
A plant 5S ribosomal RNA mimic regulates alternative splicing of
transcription factor IIIA pre-mRNAs pp541 - 549
Production of complex machines such as the ribosome requires
coordinated regulation of the components. A widely conserved plant
regulator of alternative splicing on the TFIIIA transcription factor
mRNA has been found. The RNA structurally mimics the 5S rRNA and,
accordingly, binds ribosomal protein L5, which thus affects splicing
and production of TFIIIA. As TFIIIA is needed for transcription of
the 5S rRNA, this work defines a regulatory circuit for coordinating
5S rRNA production by its binding protein.
Ming C Hammond, Andreas Wachter and Ronald R Breaker
doi:10.1038/nsmb.1588
Abstract: http://links.ealert.nature.com/ctt?kn=58&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=109&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
The nucleotide binding dynamics of human MSH2-MSH3 are lesion
dependent pp550 - 557
The Msh2-Msh3 complex recognizes DNA mismatch lesions, with stronger
affinity for small insertion and deletion loops. Now the nucleotide
binding properties of Msh2-Msh3 are studied, revealing the changes
upon binding to DNA molecules with a loop lesion, indicating how
this mismatch sensor can signal the repair machinery.
Barbara A L Owen, Walter H Lang and Cynthia T McMurray
doi:10.1038/nsmb.1596
Abstract: http://links.ealert.nature.com/ctt?kn=20&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=122&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
----------------------
BRIEF COMMUNICATIONS
----------------------
Structural basis for assembly and disassembly of the CRM1 nuclear
export complex pp558 - 560
The nuclear transport receptor CRM1 mediates protein export from the
nucleus through recognition of leucine-rich nuclear export signals
on substrates. Structural analysis, based in part on the recent
structure of a CRM1-SNUPN complex, reveal determinants for substrate
binding and suggest a mechanism for binding partner-assisted
dissociation of SNUPN in the cytoplasm.
Xiuhua Dong, Anindita Biswas and Yuh Min Chook
doi:10.1038/nsmb.1586
Abstract: http://links.ealert.nature.com/ctt?kn=13&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=56&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
The WAVE regulatory complex is inhibited pp561 - 563
WAVE proteins in the WASP family are controlled by incorporation
into the WAVE regulatory complex (WRC), which transmits information
from the Rac GTPase to the actin cytoskeleton. By reconstituting
human and fly WRCs, the native complex is shown to be inactive. Rac
activates the WRC, but does not cause subunit dissociation. These
results reconcile previous work and reveal common regulatory
principles for the WASP family.
Ayman M Ismail et al.
doi:10.1038/nsmb.1587
Abstract: http://links.ealert.nature.com/ctt?kn=10&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=66&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
----------------------
RESOURCE
----------------------
Developmental programming of CpG island methylation profiles in
the human genome pp564 - 571
Ravid Straussman et al.
doi:10.1038/nsmb.1594
Abstract: http://links.ealert.nature.com/ctt?kn=113&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=125&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
----------------------
CORRIGENDA
----------------------
Corrigendum: Telomere protection by mammalian Pot1 requires
interaction with Tpp1 p572
Dirk Hockemeyer et al.
doi:10.1038/nsmb0509-572a
http://links.ealert.nature.com/ctt?kn=116&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
Corrigendum: Integration of an electric-metal sensory experience in
the Slo1 BK channel p572
Frank T Horrigan and Toshinori Hoshi
doi:10.1038/nsmb0509-572b
http://links.ealert.nature.com/ctt?kn=94&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
=========================== ADVERTISEMENT ===========================
Special Issue on Gene Therapy for Chronic Pain
Guest Editors: Joseph Glorioso and David Fink
Volume 16 Number 4
Chronic pain is a significant medical problem. Recent studies suggest that employing gene transfer to release neuroactive peptides at targeted sites in the pain pathway may be an effective means to reduce pain, while avoiding off-target side effects that limit pharmacologic treatment. This issue surveys results from preclinical animal studies using several different vector technologies, and describes the first clinical trial of gene transfer for the treatment of pain using an HSV-based vector that began enrolling patients in December 2008.
Free content available now
http://links.ealert.nature.com/ctt?kn=103&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
=====================================================================
You have been sent this Table of Contents Alert because you have
opted in to receive it. You can change or discontinue your e-mail
alerts at any time, by modifying your preferences on your nature.com
account at:
http://links.ealert.nature.com/ctt?kn=19&m=32894819&r=MTc2OTcxOTY5MQS2&b=2&j=NDg1NDIzMDgS1&mt=1&rt=0
(You will need to log in to be recognised as a nature.com registrant).
For further technical assistance, please contact our registration
department:
registration@nature.com
For print subscription enquiries, please contact our subscription
department:
subscriptions@nature.com
For other enquiries, please contact our customer feedback department:
feedback@nature.com
Nature Publishing Group | 75 Varick Street, 9th Floor | New York |
NY 10013-1917 | USA
Nature Publishing Group's worldwide offices:
London - Paris - Munich - New Delhi - Tokyo - Melbourne -
San Diego - San Francisco - Washington - New York - Boston
(c) Copyright 2009 Nature Publishing Group
=====================================================================
