June 2009 Volume 16 Number 16, pp 573 - 676
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Focus on Protein Folding
Nature Structural & Molecular Biology presents a focus issue on
'Protein Folding', with four commissioned Reviews and one Perspective.
These will cover topics of fundamental importance to a wide range of
researchers: the role of chaperones; the experimental approaches used
to study protein folding; the ribosome as a platform for protein
processing and folding; the biology of prions; and how integral
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Nature Reviews Molecular Cell Biology
Article Series on Chromatin Dynamics
In March 2009, Nature Reviews Molecular Cell Biology launched an
Article Series that focuses on recent breakthroughs in our
understanding of the mechanisms that govern the dynamic structural
and spatial organization of chromatin, thereby providing important
insights into gene regulation, DNA repair, development and epigenetic
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EDITORIAL
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Focus on Protein Folding
Folding to function p573
The practice of origami dates from the 1600s, but this cannot
compare to how long proteins have been evolving form and function.
How proteins achieve their correct shape is the subject of this
special Focus.
doi:10.1038/nsmb0609-573
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REVIEWS
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Focus on Protein Folding
Converging concepts of protein folding in vitro and in vivo
pp574 - 581
F Ulrich Hartl and Manajit Hayer-Hartl
doi:10.1038/nsmb.1591
Abstract: http://links.ealert.nature.com/ctt?kn=116&m=33344668&r=MTc2OTcxOTY5MQS2&b=2&j=NTA3NTkxNjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=69&m=33344668&r=MTc2OTcxOTY5MQS2&b=2&j=NTA3NTkxNjMS1&mt=1&rt=0
Focus on Protein Folding
An expanding arsenal of experimental methods yields an explosion of
insights into protein folding mechanisms pp582 - 588
Alice I Bartlett and Sheena E Radford
doi:10.1038/nsmb.1592
Abstract: http://links.ealert.nature.com/ctt?kn=84&m=33344668&r=MTc2OTcxOTY5MQS2&b=2&j=NTA3NTkxNjMS1&mt=1&rt=0
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Focus on Protein Folding
The ribosome as a platform for co-translational processing, folding
and targeting of newly synthesized proteins pp589 - 597
Gunter Kramer, Daniel Boehringer, Nenad Ban and Bernd Bukau
doi:10.1038/nsmb.1614
Abstract: http://links.ealert.nature.com/ctt?kn=133&m=33344668&r=MTc2OTcxOTY5MQS2&b=2&j=NTA3NTkxNjMS1&mt=1&rt=0
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PERSPECTIVES
----------------------
Focus on Protein Folding
Unraveling infectious structures, strain variants and species
barriers for the yeast prion [PSI+] pp598 - 605
Peter M. Tessier and Susan Lindquist
doi:10.1038/nsmb.1617
Abstract: http://links.ealert.nature.com/ctt?kn=124&m=33344668&r=MTc2OTcxOTY5MQS2&b=2&j=NTA3NTkxNjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=132&m=33344668&r=MTc2OTcxOTY5MQS2&b=2&j=NTA3NTkxNjMS1&mt=1&rt=0
Focus on Protein Folding
Cellular mechanisms of membrane protein folding pp606 - 612
William R Skach
doi:10.1038/nsmb.1600
Abstract: http://links.ealert.nature.com/ctt?kn=99&m=33344668&r=MTc2OTcxOTY5MQS2&b=2&j=NTA3NTkxNjMS1&mt=1&rt=0
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NEWS AND VIEWS
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A new way to initiate mRNA degradation pp613 - 614
Removal of the poly(A) tail is the initial step in targeting an
mRNA for degradation in budding yeast as well as in metazoans.
But in fission yeast a new study reveals an additional pathway
that adds uridines to the poly(A) tail of mRNA to initiate the
degradation pathway.
William Marzluff
doi:10.1038/nsmb0609-613
http://links.ealert.nature.com/ctt?kn=102&m=33344668&r=MTc2OTcxOTY5MQS2&b=2&j=NTA3NTkxNjMS1&mt=1&rt=0
Activating apoptosis p614
Sabbi Lall
doi:10.1038/nsmb0609-614
http://links.ealert.nature.com/ctt?kn=97&m=33344668&r=MTc2OTcxOTY5MQS2&b=2&j=NTA3NTkxNjMS1&mt=1&rt=0
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RESEARCH HIGHLIGHTS
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Research highlights p615
doi:10.1038/nsmb0609-615
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ARTICLES
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Decapping is preceded by 3' uridylation in a novel pathway of
bulk mRNA turnover pp616 - 623
Turnover of mRNA has mainly been studied in the budding yeast,
Saccharomyces cerevisiae, and is thought to be initiated by
deadenylation. Now Rissland and Norbury reveal that additional,
parallel decay pathways are at work in the fission yeast,
Schizosaccharomyces pombe. They find that mRNA decapping is
frequently independent of deadenylation and that Cid1-dependent
uridylation of polyadenylated mRNAs seems to stimulate decapping
as part of a novel mRNA turnover pathway. As human cells contain
Cid1 orthologs, uridylation may form the basis of a widespread,
conserved mechanism of mRNA decay.
Olivia S Rissland and Chris J Norbury
doi:10.1038/nsmb.1601
Abstract: http://links.ealert.nature.com/ctt?kn=24&m=33344668&r=MTc2OTcxOTY5MQS2&b=2&j=NTA3NTkxNjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=107&m=33344668&r=MTc2OTcxOTY5MQS2&b=2&j=NTA3NTkxNjMS1&mt=1&rt=0
PKC maturation is promoted by nucleotide pocket occupation
independently of intrinsic kinase activity pp624 - 630
Protein kinase C epsilon (PKC epsilon) priming involves phosphorylation
of the kinase domain at 3 different sites. Whether these
phosphorylation events were autocatalytic was unclear. Now Parker
and colleagues use different PKC epsilon mutants and inhibitors to
demonstrate that the occupancy of the nucleotide binding pocket, and
not catalytic activity, promote priming of PKC epsilon.
Angus J M Cameron et al.
doi:10.1038/nsmb.1606
Abstract: http://links.ealert.nature.com/ctt?kn=17&m=33344668&r=MTc2OTcxOTY5MQS2&b=2&j=NTA3NTkxNjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=2&m=33344668&r=MTc2OTcxOTY5MQS2&b=2&j=NTA3NTkxNjMS1&mt=1&rt=0
The N-terminal domain of GluR6-subtype glutamate receptor ion channels
pp631 - 638
The amino-terminal domain (ATD) of ionotropic glutamate receptors
(iGluRs) mediates their assembly into AMPA-, kainate- and
NMDA-sensitive subtypes. The crystal structure of the ATD from the
kainate receptor GluR6 reveals a dimeric organization and likely
determinants for subtype-selective assembly.
Janesh Kumar, Peter Schuck, Rongsheng Jin and Mark L Mayer
doi:10.1038/nsmb.1613
Abstract: http://links.ealert.nature.com/ctt?kn=25&m=33344668&r=MTc2OTcxOTY5MQS2&b=2&j=NTA3NTkxNjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=131&m=33344668&r=MTc2OTcxOTY5MQS2&b=2&j=NTA3NTkxNjMS1&mt=1&rt=0
Loss of the Mili-interacting Tudor domain-containing protein-1
activates transposons and alters the Mili-associated small RNA
profile pp639 - 646
piRNAs have been implicated in transposon silencing. Tudor
domain-containing protein-1 (Tdrd1) is now shown to interact with
the mouse Piwi ortholog Mili and be part of a complex that contains
Mili-associated piRNAs. Interaction occurs through the N terminus of
Mili, which is dimethylated, a modification that promotes Tdrd1
interaction. The Tdrd1 mutant shares phenotypes with the Mili mutant
but shows a strong effect on the nature of the small RNA pool
associated with Mili.
Michael Reuter et al.
doi:10.1038/nsmb.1615
Abstract: http://links.ealert.nature.com/ctt?kn=129&m=33344668&r=MTc2OTcxOTY5MQS2&b=2&j=NTA3NTkxNjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=63&m=33344668&r=MTc2OTcxOTY5MQS2&b=2&j=NTA3NTkxNjMS1&mt=1&rt=0
Bacterial ubiquitin-like modifier Pup is deamidated and conjugated
to substrates by distinct but homologous enzymes pp647 - 651
Pupylation is the bacterial equivalent of ubiquitin conjugation, and
it involves C-terminal Pup conjugation to lysines to target proteins
for proteasomal degradation. This modification reaction has now been
reconstituted in vitro using enzymes from the pathogen Mycobacterium
tuberculosis. The Pup deamidase (Dop) of this pathway has been
defined, and PafA has been shown to conjugate deamidated Pup to
substrates.
Frank Striebel et al.
doi:10.1038/nsmb.1597
Abstract: http://links.ealert.nature.com/ctt?kn=21&m=33344668&r=MTc2OTcxOTY5MQS2&b=2&j=NTA3NTkxNjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=15&m=33344668&r=MTc2OTcxOTY5MQS2&b=2&j=NTA3NTkxNjMS1&mt=1&rt=0
Antidepressant specificity of serotonin transporter suggested by
three LeuT-SSRI structures pp652 - 657
Sertraline (Zoloft) and fluoxetine (Prozac) are selective
serotonin-reuptake inhibitors (SSRIs) that are widely prescribed
to treat depression. They bind to the presynaptic plasma membrane
serotonin transporter (SERT) and inhibit serotonin uptake. Both
these drugs possess halogen atoms, but the structural basis for
the specificity of SERT for these inhibitors was not known. Zhou
et al. now report the crystal structure of LeuT, a bacterial SERT
homolog in complex with three different SSRIs. The halogen atoms
of all three bind within exactly the same pocket of LeuT, and
mutations within this pocket in SERT markedly reduce the
transporter's affinity for SSRIs but not for tricyclic
antidepressants.
Zheng Zhou et al.
doi:10.1038/nsmb.1602
Abstract: http://links.ealert.nature.com/ctt?kn=11&m=33344668&r=MTc2OTcxOTY5MQS2&b=2&j=NTA3NTkxNjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=121&m=33344668&r=MTc2OTcxOTY5MQS2&b=2&j=NTA3NTkxNjMS1&mt=1&rt=0
E2 interaction and dimerization in the crystal structure of TRAF6
pp658 - 666
The signaling adaptor TRAF6 is a ubiquitin E3 ligase whose activity
can lead to activation of NF-kappa B and MAPK pathways. New data
based on the structure of TRAF6 in complex with the ubiquitin E2
Ubc13 suggest that other TRAFs do not interact with Ubc13 and that
oligomerization of TRAF6 is needed for downstream signal transduction.
Qian Yin et al.
doi:10.1038/nsmb.1605
Abstract: http://links.ealert.nature.com/ctt?kn=12&m=33344668&r=MTc2OTcxOTY5MQS2&b=2&j=NTA3NTkxNjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=138&m=33344668&r=MTc2OTcxOTY5MQS2&b=2&j=NTA3NTkxNjMS1&mt=1&rt=0
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BRIEF COMMUNICATION
----------------------
Structural insight into the quinolone-DNA cleavage complex of type
IIA topoisomerases pp667 - 669
Topoisomerases alter DNA topology, an essential activity in all
organisms. Bacterial type II topoisomerases are targets for
antimicrobials such as quinolones, whose binding mode was unclear.
Now the crystal structures of pneumococcal topoisomerase IV in a DNA
cleavage complex bound to moxifloxacin or clinafloxacin provide
insight into how these drugs work and how bacteria can acquire
resistance.
Ivan Laponogov et al.
doi:10.1038/nsmb.1604
Abstract: http://links.ealert.nature.com/ctt?kn=118&m=33344668&r=MTc2OTcxOTY5MQS2&b=2&j=NTA3NTkxNjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=26&m=33344668&r=MTc2OTcxOTY5MQS2&b=2&j=NTA3NTkxNjMS1&mt=1&rt=0
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RESOURCE
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Cancer-associated regulation of alternative splicing pp670 - 676
Julian P Venables et al.
doi:10.1038/nsmb.1608
Abstract: http://links.ealert.nature.com/ctt?kn=114&m=33344668&r=MTc2OTcxOTY5MQS2&b=2&j=NTA3NTkxNjMS1&mt=1&rt=0
Article: http://links.ealert.nature.com/ctt?kn=88&m=33344668&r=MTc2OTcxOTY5MQS2&b=2&j=NTA3NTkxNjMS1&mt=1&rt=0
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