September 2008 Volume 15 Number 9, pp 889 - 998
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----------------------
EDITORIAL
----------------------
It takes time p889
A look at the editorial process indicates why having your paper
reviewed might take some time.
doi:10.1038/nsmb0908-889
http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vC0EK
----------------------
CORRESPONDENCE
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The binding stoichiometry of CIN85 SH3 domain A and Cbl-b
pp890 - 891
Abdessamad Ababou, Mark Pfuhl and John E Ladbury
doi:10.1038/nsmb0908-890
http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vD0EL
Reply to "The binding stoichiometry of CIN85 SH3 domain A and Cbl-b"
pp891 - 892
Daniela Jozic et al.
doi:10.1038/nsmb0908-891
http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vE0EM
----------------------
NEWS AND VIEWS
----------------------
Insights into PPARgamma from structures with endogenous and
covalently bound ligands pp893 - 895
Peroxisome proliferator-activated receptor-gamma (PPARgamma) is a
ligand-regulated transcription factor with crucial roles in
carbohydrate and lipid metabolism and adipogenesis, but the
structural details of the binding and activation by endogenous
ligands are not known. Two recent studies reveal how oxidized and
nitrated fatty acids uniquely bind and activate PPARgamma.
Kendall W Nettles
doi:10.1038/nsmb0908-893
http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vF0EN
How does Plasmodium falciparum stick to CSA? Let's see in the crystal
pp895 - 897
The crystal structure of the CSA-binding Duffy-binding-like domain
DBL3x of the VAR2CSA-encoded PfEMP1 adhesin has been solved in the
free state and complexed with CSA oligosaccharides, shedding light
on the major host-parasite interaction in pregnancy-associated
malaria.
Graham A Bentley and Benoit Gamain
doi:10.1038/nsmb0908-895
http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vG0EO
A new, leaner and meaner bacterial organelle pp897 - 898
Bacteria sequester key metabolic steps into polyhedral protein
compartments. A newly discovered nanocompartment reveals what it
takes for its cargo protein to become encapsulated within a protein
shell.
Sabine Heinhorst and Gordon C Cannon
doi:10.1038/nsmb0908-897
http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vH0EP
Sister chromatids caught in the cohesin trap pp899 - 900
Cohesin is a large ring-shaped protein complex that mediates cohesion
between sister chromatids. New experiments show that the sister
chromatids of a minichromosome are entrapped by monomeric cohesin
rings, thus excluding the possibility that sister chromatid cohesion
is mediated by nontopological interactions between cohesin complexes.
Lubos Cipak, Mario Spirek and Juraj Gregan
doi:10.1038/nsmb0908-899
http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vI0EQ
----------------------
RESEARCH HIGHLIGHTS
----------------------
Research highlights p901
doi:10.1038/nsmb0908-901
http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vJ0ER
----------------------
ARTICLES
----------------------
Primary microRNA transcripts are processed co-transcriptionally
pp902 - 909
MicroRNAs are processed by Drosha, and previous data had suggested
that this occurred soon after transcription. Following Drosha
recruitment and using nuclear run-on technology, data now indicate
that miRNAs both within and outside of introns are processed
co-transcriptionally and that exonucleases enter the fray to aid
processing before splicing, implying that Drosha cleavage influences
the maturation of the pre-mRNAs in which miRNAs reside.
Mariangela Morlando et al.
doi:10.1038/nsmb.1475
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vK0ES
Article: http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vL0ET
A new tRNA intermediate revealed on the ribosome during EF4-mediated
back-translocation pp910 - 915
The ribosomal GTPase, LepA or EF4, can promote back-translocation of
tRNAs, thus reversing translocation. The cryo-EM structure of the
ribosome with EF4 now suggests how such back-translocation can be
allowed to occur and reveals that the tRNA is in an intermediate
state that deviates from its canonical position.
Sean R Connell et al.
doi:10.1038/nsmb.1469
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vM0EU
Article: http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vN0EV
SRP RNA controls a conformational switch regulating the SRP-SRP
receptor interaction pp916 - 923
The interaction between the signal-recognition particle (SRP) and
its receptor (SR) is catalyzed by the RNA component of SRP, but the
mechanism is not clear. Now, kinetics and NMR studies reveal an
inhibitory role of the N-terminal helices of both proteins,
suggesting that the RNA facilitates formation of the SRP-SR complex
by promoting conformational changes of these helices.
Saskia B Neher et al.
doi:10.1038/nsmb.1467
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vO0EW
Article: http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vP0EX
Structural basis for the activation of PPARgamma by oxidized fatty acids
pp924 - 931
PPARgamma is a nuclear receptor that regulates metabolic homeostasis
and whose physiological ligands are nitrated and oxidized fatty
acids. The crystal structures of the ligand binding domain of
PPARgamma in complex with several oxidized fatty acids are now
described, showing differences with synthetic agonists that may
have physiological relevance.
Toshimasa Itoh et al.
doi:10.1038/nsmb.1474
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vQ0EY
Article: http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vR0EZ
Structure of the DBL3x domain of pregnancy-associated malaria
protein VAR2CSA complexed with chondroitin sulfate A pp932 - 938
In pregnancy-associated malaria, parasite-infected erythrocytes
express the protein VAR2CSA on their surface and bind to chondroitin
sulfate A in the placenta, with severe effects to the mother and the
fetus. Now the crystal structure of a domain of VAR2CSA in complex
with chondroitin sulfate A is reported and, together with functional
studies, sheds insight into this interaction.
Kavita Singh et al.
doi:10.1038/nsmb.1479
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vS0Ea
Article: http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vT0Eb
Structural basis of enzyme encapsulation into a bacterial
nanocompartment pp939 - 947
Certain bacterial enzymes are packaged within protein chambers that
provide a confined environment for their reactions to take place.
Ban and colleagues now identify a family of proteins that form
nanocompartments, similar to bacterial microcompartments such as
the carboxysome, and show that the enzymes within are anchored by
their C-terminal extensions to binding sites on the inner surface
of the chamber.
Markus Sutter et al.
doi:10.1038/nsmb.1473
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vU0Ec
Article: http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vV0Ed
Molecular functions of the histone acetyltransferase chaperone
complex Rtt109-Vps75 pp948 - 956
Vps75 is a histone chaperone that associates with the Rtt109
acteyltransferase. The structure of Vps75 and further biochemical
analysis suggest how Vps75 functions to alter histone H3K9
acetylation during S phase, and suggest a model for how it activates
the histone acetyltransferase.
Christopher E Berndsen et al.
doi:10.1038/nsmb.1459
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vW0Ee
Article: http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vX0Ef
Histone chaperone specificity in Rtt109 activation pp957 - 964
The structure of yeast Vps75, a histone chaperone that associates
with the Rtt109 histone acetyltransferase, is presented and compared
to Nap1, which interacts with the same histone acetyltransferase.
Young-Jun Park et al.
doi:10.1038/nsmb.1480
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vY0Eg
Article: http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vZ0Eh
A regulatable switch mediates self-association in an immunoglobulin
fold pp965 - 971
Formation of beta-2 microglobulin (beta2m) amyloid fibrils is
associated with dialysis-related amyloidosis. beta2m pre-amyloid
formation occurs in a Cu2+-dependent manner in vitro. Structural
studies reveal that structural changes away from the Cu2+ binding
site create conditions that promote beta2m oligomerization
leading to amyloidogenesis.
Matthew F Calabrese, Catherine M Eakin, Jimin M Wang and Andrew D Miranker
doi:10.1038/nsmb.1483
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4va0Eo
Article: http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vb0Ep
The HP1-p150/CAF-1 interaction is required for pericentric
heterochromatin replication and S-phase progression in mouse cells
pp972 - 979
The architecture of heterochromatin is maintained by HP1, which is
known to interact with the p150 subunit from the histone chaperone
complex CAF-1. This interaction is now shown to be important for the
replication of pericentric heterochromatin regions during late S
phase in mouse cells, a role that is independent of CAF-1's
histone-deposition activity.
Jean-Pierre Quivy et al.
doi:10.1038/nsmb.1470
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vc0Eq
Article: http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vd0Er
Structural basis for group A trichothiodystrophy pp980 - 984
Group A trichothiodystrophy is caused by mutations in the p8 subunit
of the TFIIH complex, involved in transcription and
nucleotide-excision repair. Now the structure of the yeast ortholog
of p8 in complex with a fragment of the yeast ortholog of p52 shows
how p8 stabilizes p52 and thus the whole TFIIH complex.
Denis E Kainov et al.
doi:10.1038/nsmb.1478
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4ve0Es
Article: http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vf0Et
A proposed OB-fold with a protein-interaction surface in Candida
albicans telomerase protein Est3 pp985 - 989
The Est3 telomerase subunit has a critical, but still uncharacterized
regulatory role in yeast telomere maintenance. An OB-fold is now
predicted for Candida albicans Est3 protein, and residues important
for its association with the telomerase complex are identified.
Eun Young Yu, Feng Wang, Ming Lei and Neal F Lue
doi:10.1038/nsmb.1471
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vg0Eu
Article: http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vh0Ev
The Est3 protein associates with yeast telomerase through an OB-fold
domain pp990 - 997
The Est3 telomerase subunit has a critical, but still uncharacterized
regulatory role in yeast telomere maintenance. An OB-fold is now
predicted for Saccharomyces cerevisiae Est3 protein, and residues
important for its association with the telomerase complex are
identified.
Jaesung Lee et al.
doi:10.1038/nsmb.1472
Abstract: http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vi0Ew
Article: http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vj0Ex
----------------------
CORRIGENDA
----------------------
Single-molecule studies of fork dynamics in Escherichia coli DNA
replication p998
Nathan A Tanner et al.
doi:10.1038/nsmb0908-998a
http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vk0Ey
A mammalian microRNA cluster controls DNA methylation and telomere
recombination via Rbl2-dependent regulation of DNA methyltransferases
p998
Roberta Benetti et al.
doi:10.1038/nsmb0908-998b
http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vl0Ez
Two distinct mechanisms generate endogenous siRNAs from bidirectional
transcription in Drosophila melanogaster p998
Katsutomo Okamura et al.
doi:10.1038/nsmb0908-998c
http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vm0E1
Fungal Rtt109 histone acetyltransferase is an unexpected structural
homolog of metazoan p300/CBP p998
Yong Tang et al.
doi:10.1038/nsmb0908-998d
http://ealerts.nature.com/cgi-bin24/DM/y/enLn0Xztnp0Hjh0B4vn0E2
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