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World Stem Cell Summit 2010

Thursday, August 6, 2009

Nature Structural & Molecular Biology Contents: August 2009 Volume #16 pp 797 - 897

NATURE STRUCTURAL & MOLECULAR BIOLOGY

August 2009 Volume 16 Number 8, pp 797 - 897

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----------------------
EDITORIAL
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A different perspective on science p797
A recent survey revealed striking differences between the public
and scientists' views of US scientific achievement and its societal
benefits. This reinforces the fact that more must be done to
effectively communicate with, educate and engage the public.
doi:10.1038/nsmb0809-797
http://links.ealert.nature.com/ctt?kn=8&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0

----------------------
NEWS AND VIEWS
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Mre11: roles in DNA repair beyond homologous recombination
pp798 - 800
The Mre11 protein has well-documented functions in the repair of
DNA double-strand breaks via homologous recombination. Now, several
new studies reveal that Mre11 also has a role in mammalian DNA
double-strand break repair by nonhomologous end joining.
Shan Zha, Cristian Boboila and Frederick W Alt
doi:10.1038/nsmb0809-798
http://links.ealert.nature.com/ctt?kn=93&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0

Hit and run: X marks the spot! pp801 - 803
Male fruitflies upregulate transcription of nearly all genes on their
single X chromosome to equalize expression with the two X chromosomes
in females. A new study shows that the distribution of the histone
acetylation mark associated with this upregulation is much broader
than that of the MSL complex responsible for depositing this mark.
Vikki M Weake and Jerry L Workman
doi:10.1038/nsmb0809-801
http://links.ealert.nature.com/ctt?kn=48&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0

Grb-ing hold of insulin signaling pp803 - 804
It is just as important to shut off a signaling pathway as it is to
turn it on. A new study on the tandem Ras-associating (RA) and
pleckstrin-homology (PH) domains of Grb10 and Grb14 provides
important insight into a multicomponent assembly for downregulating
insulin receptor signaling.
Derek F J Ceccarelli and Frank Sicheri
doi:10.1038/nsmb0809-803
http://links.ealert.nature.com/ctt?kn=91&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0

Kill the messenger: bacterial antisense RNA promotes mRNA decay
pp804 - 806
Bacterial antisense RNAs target translation initiation regions
(TIRs) to compete with ribosome binding, thus repressing translation
and-secondarily-causing degradation of the naked mRNA.
A new study reports on an antisense RNA that directly accelerates
mRNA decay by targeting a sequence deep within the coding region,
far downstream of the TIR.
E Gerhart H Wagner
doi:10.1038/nsmb0809-804
http://links.ealert.nature.com/ctt?kn=37&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0

----------------------
RESEARCH HIGHLIGHTS
----------------------
Research highlights p807
doi:10.1038/nsmb0809-807
http://links.ealert.nature.com/ctt?kn=69&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0

----------------------
ARTICLES
----------------------
Multiple functions of MRN in end-joining pathways during isotype
class switching pp808 - 813
The MRN complex is known to have a role in the cellular response
to DNA double-strand breaks in mammals, particularly in damage
signaling, checkpoint responses and homologous recombination. Now
MRN is found to function in nonhomologous end joining during mouse
class switch recombination.
Maria Dinkelmann et al.
doi:10.1038/nsmb.1639
Abstract: http://links.ealert.nature.com/ctt?kn=113&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=43&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0

Role of mammalian Mre11 in classical and alternative nonhomologous
end joining pp814 - 818
The MRN complex is known to have a role in the cellular response
to DNA double-strand breaks in higher eukaryotes, particularly in
damage signaling and checkpoint responses and homologous
recombination. Now MRN is found to function in nonhomologous end
joining in murine stem cells.
Anyong Xie, Amy Kwok and Ralph Scully
doi:10.1038/nsmb.1640
Abstract: http://links.ealert.nature.com/ctt?kn=15&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=80&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0

Role of Mre11 in chromosomal nonhomologous end joining in mammalian
cells pp819 - 824
The MRN complex is known to play a role in the cellular response to
DNA double-strand breaks in higher eukaryotes, particularly in damage
signaling and checkpoint responses and homologous recombination. Now
MRN is found to function in non-homologous end-joining in human and
hamster cell lines.
Emilie Rass et al.
doi:10.1038/nsmb.1641
Abstract: http://links.ealert.nature.com/ctt?kn=105&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=68&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0

Drosophila MSL complex globally acetylates H4K16 on the male X
chromosome for dosage compensation pp825 - 832
Male Drosophila X chromosomes are highly transcribed to achieve
dosage parity with females. This process is mediated by the MSL
complex, though binding has been detected at only a subset of X
chromosomal loci. MSL-dependent histone H4K16 acetylation is now
found across the male X, suggesting widespread, but transient,
MSL function.
Marnie E Gelbart et al.
doi:10.1038/nsmb.1644
Abstract: http://links.ealert.nature.com/ctt?kn=112&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=56&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0

Structural and functional studies of the Ras-associating and
pleckstrin-homology domains of Grb10 and Grb14 pp833 - 839
Grb10 and Grb14 are adaptor proteins that inhibit insulin signaling
through direct interactions with the insulin receptor kinase domain.
Structural and functional studies now reveal that the tandem
Ras-associating and pleckstrin-homology domains of these proteins
are necessary for membrane recruitment and insulin receptor inhibition.
Rafael S Depetris, Jinhua Wu and Stevan R Hubbard
doi:10.1038/nsmb.1642
Abstract: http://links.ealert.nature.com/ctt?kn=86&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=81&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0

Coding sequence targeting by MicC RNA reveals bacterial mRNA
silencing downstream of translational initiation pp840 - 846
Bacterial small RNAs are generally thought to repress mRNAs at the
level of translational initiation by binding in the 5' untranslated
region. Salmonella typhimurium MicC is now shown to target the ompD
mRNA coding region, triggering decay without affecting translational
initiation.
Verena Pfeiffer et al.
doi:10.1038/nsmb.1631
Abstract: http://links.ealert.nature.com/ctt?kn=92&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=39&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0

Intrinsic histone-DNA interactions are not the major determinant of
nucleosome positions in vivo pp847 - 852
Nucleosomes can affect and be affected by processes targeting DNA.
By comparing the in vitro positions of assembled nucleosomes on yeast
DNA with in vivo positions, it is now concluded that intrinsic
histone-DNA interactions are not the major determinant of nucleosome
positioning in vivo.
Yong Zhang et al.
doi:10.1038/nsmb.1636
Abstract: http://links.ealert.nature.com/ctt?kn=88&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=51&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0

Structural insights into host GTPase isoform selection by a family of
bacterial GEF mimics pp853 - 860
Map belongs to a family of bacterial type III effectors that can
regulate host cytoskeletal dynamics. Structural and biochemical data
reveal that Map acts as a potent GEF for the GTPase Cdc42 and suggest
how these effector molecules discriminate between target GTPases in
their host.
Zhiwei Huang et al.
doi:10.1038/nsmb.1647
Abstract: http://links.ealert.nature.com/ctt?kn=85&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=102&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0

Translation factors direct intrinsic ribosome dynamics during
translation termination and ribosome recycling pp861 - 868
The effects of translation factors on ribosome dynamics help drive
protein synthesis. The ribosome was previously shown to fluctuate
between two coordinated structural states during elongation. The
effects of release and ribosome recycling factors on this
conformational equilibrium are now examined.
Samuel H Sternberg et al.
doi:10.1038/nsmb.1622
Abstract: http://links.ealert.nature.com/ctt?kn=9&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=14&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0

Incision-dependent and error-free repair of (CAG)n/(CTG)n hairpins in
human cell extracts pp869 - 875
CAG/CTG trinucleotide repeat expansion is linked to disorders such
as Huntington's disease. These repeats tend to form stable hairpins
that contribute to expansion. Removal of such DNA hairpins in human
cell extracts is now found to occur via endonucleolytic incisions in
an error-free manner followed by DNA synthesis.
Caixia Hou, Nelson L S Chan, Liya Gu and Guo-Min Li
doi:10.1038/nsmb.1638
Abstract: http://links.ealert.nature.com/ctt?kn=19&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=83&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0

Structural and functional analyses of minimal phosphopeptides
targeting the polo-box domain of polo-like kinase 1 pp876 - 882
The Plk1 kinase is a major regulator of mitosis that is often
overexpressed in human cancers. Studies on phosphopeptide inhibitors
specific to the polo-box domain of Plk1 reveal the determinants for
specificity and may provide insight into the development of new
therapeutics targeting protein-protein interactions.
Sang-Moon Yun et al.
doi:10.1038/nsmb.1628
Abstract: http://links.ealert.nature.com/ctt?kn=94&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=64&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0

Avid interactions underlie the Lys63-linked polyubiquitin binding
specificities observed for UBA domains pp883 - 889
Ubiquitin-associated (UBA) domains mediate diverse signaling events,
and minimal UBA domains have been thought to harbor a range of
polyubiquitin linkage specificities. Data now indicate that this may
not be the case, but that specificity can arise through avid interactions
with clusters of UBA domains.
Joshua J Sims et al.
doi:10.1038/nsmb.1637
Abstract: http://links.ealert.nature.com/ctt?kn=13&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=77&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0

Diversity of chemical mechanisms in thioredoxin catalysis revealed by
single-molecule force spectroscopy pp890 - 896
Thioredoxins (Trxs) reduce disulfide bonds via a Michaelis-Menten
mechanism. Upon substrate stretching at high forces, an SN2 reaction
can be used by bacterial Trxs. A third mechanism, single-electron
transfer, is now revealed in Trxs of either bacterial or eukaryotic
origin, and is correlated with the depth of the Trx substrate-binding
groove.
Raul Perez-Jimenez et al.
doi:10.1038/nsmb.1627
Abstract: http://links.ealert.nature.com/ctt?kn=1&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=17&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0

----------------------
CORRIGENDUM
----------------------
Corrigendum: Three-dimensional reconstruction of the Shigella T3SS
transmembrane regions reveals 12-fold symmetry and novel features
throughout p897
Julie L Hodgkinson et al.
doi:10.1038/nsmb0809-897b
http://links.ealert.nature.com/ctt?kn=99&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0

----------------------
ERRATUM
----------------------
Erratum: The nucleotide binding dynamics of human MSH2-MSH3 are
lesion dependent p897
Barbara A L Owen, Walter H Lang and Cynthia T McMurray
doi:10.1038/nsmb0809-897a
http://links.ealert.nature.com/ctt?kn=76&m=33815051&r=MTc2OTcxOTY5MQS2&b=2&j=NTUxODk1NjMS1&mt=1&rt=0

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