NATURE AND THE NATURE RESEARCH JOURNALS PRESS RELEASE
For papers that will be published online on 20 November 2005
This press release is copyrighted to the Nature journals mentioned below.
This press release contains:
* Summaries of newsworthy papers:
* A magnetic discovery about bacteria - Nature
* Molecules that suck - Nature Materials
* Blocking protein secretion - Nature Chemical Biology
* Activating Smoothened - Nature Chemical Biology
* A silent killer - Nature Neuroscience
* Perfect fit for immune recognition - Nature Immunology
* DISC1, neuronal development and schizophrenia - Nature Cell Biology
* Mention of papers to be published at the same time with the same embargo
* Paper(s) for immediate release
* Geographical listing of authors
PDFs of all the papers mentioned on this release can be found in the
relevant journal's section of http://press.nature.com. Press contacts for
the Nature journals are listed at the end of this release.
Warning: This document, and the Nature journal papers to which it refers,
may contain information that is price sensitive (as legally defined, for
example, in the UK Criminal Justice Act 1993 Part V) with respect to
publicly quoted companies. Anyone dealing in securities using information
contained in this document, or in advance copies of a Nature journal's
content, may be guilty of insider trading under the US Securities Exchange
Act of 1934.
PICTURES: To obtain artwork from any of the journals, you must first obtain
permission from the copyright holder (if named) or author of the research
paper in question (if not).
NOTE: Once a paper is published, the digital object identifier (DOI) number
can be used to retrieve the abstract and full text from the journal web site
(abstracts are available to everyone, full text is available only to
subscribers). To do this, add the DOI to the following URL:
<http://dx.doi.org/> (For example, <http://dx.doi.org/10.1038/ng730>). For
more information about DOIs and Advance Online Publication, see
<http://www.nature.com/ng/aop/>.
PLEASE CITE THE SPECIFIC NATURE JOURNAL AND WEBSITE AS THE SOURCE OF THE
FOLLOWING ITEMS. IF PUBLISHING ONLINE, PLEASE CARRY A HYPERLINK TO THE
APPROPRIATE JOURNAL'S WEBSITE.
********************************NATURE*********************************
(<http://www.nature.com/nature>)
[1] A magnetic discovery about bacteria
DOI: 10.1038/nature04382
Magnetotactic bacteria are aquatic microorganisms that use unique organelles
called magnetosomes to navigate along the Earth's magnetic field. Much of
the biochemistry behind magnetosome structures has eluded scientists, but a
paper published online by Nature describes how an acidic protein helps to
align magnetosomes in the cell.
Dirk Schüler and his colleagues used gene deletion in a magnetotactic
bacterium called Magnetospirillum gryphiswaldense to show the important role
of the MamJ protein. This acidic protein seems to influence how chains of
magnetite crystals form and remain stable within the cell. The authors also
provide the first direct evidence for a novel cytoskeletal structure that
anchors these chains, and suggest that magnetosome architecture represents
one of the highest levels of structure in bacterial cells.
Author contact:
Dirk Schuler (Max Planck Institute for Marine Microbiology, Bremen, Germany)
Tel: +49 421 2028 7546, E-mail: [email protected]
Other papers from Nature to be published online at the same time and with
the same embargo:
[2] A phosphatase complex that dephosphorylates gammaH2AX regulates DNA
damage checkpoint recovery
DOI: 10.1038/nature04384
**************************NATURE MATERIALS************************
(<http://www.nature.com/naturematerials>)
[3] Molecules that suck
DOI: 10.1038/nmat1529
The interaction between the tip of a scanning tunnelling microscope (STM)
and atoms or molecules bound to a surface can be used to construct
impressive nanostructures, such as the 'quantum corral'. As reported in the
December issue of Nature Materials, researchers combine STM manipulation
techniques with the ability of a molecule to assemble nanostructures by
sucking up and depositing atoms where needed.
The invention of the STM in the early 1980s was the catalyst of the
nanoscale technological revolution, not only for imaging but also for
interacting with matter at the atomic scale. Since then, progress in
manipulation techniques has shown that the interaction of molecules with the
surface of a metal can induce surface reconstruction. Francesca Moresco and
colleagues now go a step further by moving and organizing metal atoms on a
substrate with the help of a well-designed six-leg organic molecule.
The copper atoms trapped under the organic molecule can be further
rearranged by bringing the whole system and its copper load to a specific
position on the surface where the metal atoms can subsequently be released.
The authors believe that this versatile assembling approach should
facilitate the interconnection of molecular devices to well-defined
atomic-scale metallic electrodes on insulating surfaces, where STM has so
far proved unsuccessful.
Author contact:
Francesca Moresco (Freie Universität Berlin, Germany)
Tel: +49 308 385 1355, E-mail: [email protected]
Other papers from Nature Materials to be published online at the same time
and with the same embargo:
[4] Relationships between supercontraction and mechanical properties of
spider silk
DOI: 10.1038/nmat1534
[5] Optical gain and stimulated emission in periodic nanopatterned
crystalline silicon
DOI: 10.1038/nmat1530
[6] Diffractive electron imaging of nanoparticles on a substrate
DOI: 10.1038/nmat1531
[7] Light-induced gene transfer from packaged DNA enveloped in a dendrimeric
photosensitizer
DOI: 10.1038/nmat1524
*********************NATURE CHEMICAL BIOLOGY************************
(http://www.nature.com/nchembio)
[8] Blocking protein secretion
DOI: 10.1038/nchembio751
A new class of protein secretion inhibitors, which will provide a novel
route for studying the basic biology of protein secretion, is reported in
the January issue of Nature Chemical Biology. Proteins that will ultimately
be secreted from a cell are shuttled through different organelles inside the
cell to the plasma membrane. It is difficult to study this intracellular
process by biochemical or genetic techniques because it happens relatively
quickly. Small-molecules, which are inherently fast acting, can rapidly
block specific steps in the process and thus provide an important approach
for understanding protein secretion.
Shair, Kirchhausen and colleagues have now identified a class of
small molecules, secramines, that inhibit protein movement out of an
intracellular organelle involved in protein secretion, called the golgi.
Rather than blocking activity, a more typical mechanism of inhibition,
secramines acted by preventing the movement of a protein called Cdc42 to the
golgi membrane by stabilizing an interaction between Cdc42 and a protein
inhibitor.
These chemical inhibitors now provide an important new tool for
investigating the role of Cdc42 in protein secretion and may reveal
unexpected roles for Cdc42 in other cellular processes.
Author contact:
Thomas Kirchhausen (Harvard University Medical School, Boston, MA, USA)
Tel: +1 617 278 3140, E-mail: [email protected]
Matthew Shair (Harvard University, Cambridge, MA, USA)
Tel: +1 617 495 5008, E-mail: [email protected]
[9] Activating Smoothened
DOI: 10.1038/nchembio753
The protein target of a small molecule known to induce stem cell
differentiation is reported in a paper in the January issue of Nature
Chemical Biology. This molecule, purmorphamine, has been shown to trigger
progenitor cell differentiation to osteoblasts, cells that build bones.
Purmorphamine was believed to target the Hedgehog signaling pathway, which
is involved in many developmental and growth processes in multicellular
organisms, including embryonic patterning, tissue regeneration, stem cell
renewal and cancer growth. However, the precise target of purmorphamine was
not known.
By using a combination of genetics and biochemistry, James Chen and
colleagues gradually narrowed down potential targets in the Hedgehog
signaling pathway to identify the protein Smoothened as the target. The
authors further show that purmorphamine binds directly to a bundle of
membrane-spanning helices. However even with this information about the
binding site, future studies will be necessary to characterize the precise
mechanism for how purmorphamine activates Smoothened.
Because the Hedgehog signaling pathway is involved in many critical
developmental processes and diseases, understanding the mechanism of action
of this chemical modulator provides a new lead for developing therapeutics
for certain cancers, such as brain tumors, and stem cell treatments, such as
bone regeneration.
Author contact:
James Chen (Stanford University, CA, USA)
Tel: +1 650 725 3582, E-mail: [email protected]
***************************NATURE NEUROSCIENCE************************
(<http://www.nature.com/natureneuroscience>)
[10] A silent killer
DOI: 10.1038/nn1570
A mechanism that may selectively silence the electrical activity of dopamine
producing neurons is suggested in a paper in December's Nature Neuroscience.
The slowed movements, rigidity and tremor in Parkinson's disease are caused
by a reduction in the neurotransmitter dopamine, following the death of
certain dopamine-producing neurons. What makes these neurons particularly
vulnerable is not known, but this newly observed silencing could ultimately
reduce their survival.
A common observation in Parkinson's disease and its animal models is reduced
activity of the cell's power plants, the mitochondria, which produce energy
in the form of a molecule called ATP. Birgit Liss and colleagues report that
reduced levels of ATP decreased the electrical activity of the vulnerable
neurons more strongly than in other neurons that do not die in the disease.
The electrical silencing depended on an electrical current normally
inhibited by ATP. Toxins that reduce mitochondrial function, which are used
to produce animal models of Parkinson's disease, also silenced the
vulnerable neurons. Compared to normal mice, mice genetically altered to
lack the ATP-sensitive current showed less neuron death in response to these
toxins. These results suggest that silencing of electrical activity in these
neurons might contribute to their selective vulnerability in Parkinson
disease and its animal models.
Author contact:
Birgit Liss (Marburg University, Germany)
Tel: +49 6421 286 6582, E-mail: [email protected]
Other papers from Nature Neuroscience to be published online at the same
time and with the same embargo:
[11] Prior experience of rotation is not required for recognizing objects
seen from different angles
DOI: 10.1038/nn1600
[12] The prolactin-releasing peptide antagonizes the opioid system through
its receptor GPR10
DOI: 10.1038/nn1585
[13] NMDA receptors regulate developmental gap junction uncoupling via CREB
signaling
DOI: 10.1038/nn1588
[14] Conditional dendritic spike propagation following distal synaptic
activation of hippocampal CA1 pyramidal neurons
DOI: 10.1038/nn1599
**************************NATURE IMMUNOLOGY***********************
(<http://www.nature.com/natureimmunology>)
[15] Perfect fit for immune recognition
DOI: 10.1038/ni1286
Mice lacking a particular enzyme exhibit abnormal immune responses,
resulting from a less than perfect fit of protein bits displayed to immune
cells, according to a paper in January's Nature Immunology. Nilabh Shastri
and colleagues show that mice lacking the enzyme ERAAP fail to cleave
antigenic proteins properly. Their results suggest immune cell recognition
of tumors or virally infected cells might depend on ERAAP activity.
The immune system is constantly on the lookout for sick cells.
Immune cells distinguish healthy cells from infected or abnormal cells by
the array of peptides (small bits of protein) displayed on their surface by
specialized molecules known as major histocompatibility complex (MHC)
proteins. First recognized as important for tissue matching in
transplantation studies, MHC proteins present snapshots of the protein
repertoire found inside the cell. This 'peptide presentation' involves
coordinated cleavage of cellular proteins into peptides and loading of this
peptide cargo into a groove found on the MHC molecule, whereupon peptide-MHC
complexes travel to the cell surface where they are 'sampled' by the
circulating immune cells.
ERAAP, which stands for "endoplasmic reticulum aminopeptidase associated
with antigen processing", trims peptides in the ER and thereby allows
peptides to 'fit' better in the MHC groove. Shastri and colleagues show loss
of ERAAP decreases the stability of peptide-MHC interactions, which results
in less MHC expressed on cell surfaces and those MHC molecules that do make
it to the surface readily lose their peptide cargo or display altered
peptide repertoires. ERAAP-deficient mice mount weaker immune responses to
foreign antigens. ERAAP can thus be considered as a quality control enzyme
required for proper immune cell recognition.
Author contact:
Nilabh Shastri (University of California Berkeley, CA, USA)
Tel: +1 510 643 9197, E-mail: [email protected]
************************NATURE CELL BIOLOGY***********************
(<http://www.nature.com/naturecellbiology>)
[16] DISC1, neuronal development and schizophrenia
DOI: 10.1038/ncb1328
A change in the function of a protein in the cerebral cortex may contribute
to the subtle neuronal defects observed in the brains of patients with
schizophrenia, according to a paper in the December issue of Nature Cell
Biology.
Such small changes in the brain's architecture are thought to be
contributing factors in the development of the disease and here Akira Sawa
and colleagues find that the DISC1 gene is part of a protein complex that is
important for the normal movement of cells within the brain cortex during
development.
The DISC1 gene is known to reside near the region of the chromosome
which is broken, or 'translocated', in several schizophrenia patients from a
particular Scottish pedigree. The gene binds to this complex of factors -
dynein, LIS1 and NUDEL - and recruits them to the correct location in the
cell. When the mutant form of DISC1 is present, as occurs in some
schizophrenia patients, this complex no longer reaches the appropriate
location. This complex is known to be important for normal neuronal growth
in cell culture and for neuronal cells to migrate normally within the
developing cortex. Sawa and colleagues now find that in the absence of
DISC1, or when the mutant form of DISC1 is present, cell movement in the
developing cerebral cortex is altered.
Together, these results suggest that DISC1 is important for normal formation
of the cortex, through its effects on this complex, and that this function
may be one reason neuronal development goes awry in a subset of
schizophrenia patients.
Author contact:
Akira Sawa (Johns Hopkins University, Baltimore, MD, USA)
Tel: +1 410 955 4726, E-mail: [email protected]
Other papers from Nature Cell Biology to be published online at the same
time and with the same embargo:
[17] Loading history determines the velocity of actin-network growth
DOI: 10.1038/ncb1336
[18] mPins modulates PSD-95 and SAP102 trafficking and influences NMDA
receptor surface expression
DOI: 10.1038/ncb1325
[19] Prevention of early flowering by expression of FLOWERING LOCUS C
requires methylation of histone H3 K36
DOI: 10.1038/ncb1329
**************************************************************
Items from other Nature journals to be published online at the same time and
with the same embargo:
Nature MEDICINE (<http://www.nature.com/naturemedicine>)
[20] Host-reactive CD8+ memory stem cells in graft-versus-host disease
DOI: 10.1038/nm1326
[21] Stem cells in the hair follicle bulge contribute to wound repair but
not to homeostasis of the epidermis
DOI: 10.1038/nm1328
[22] AIDS restriction HLA allotypes target distinct intervals of HIV-1
pathogenesis
DOI: 10.1038/nm1333
[23] Inhibiting Stat3 signaling in the hematopoietic system elicits
multicomponent antitumor immunity
DOI: 10.1038/nm1325
Nature BIOTECHNOLOGY (http://www.nature.com/naturebiotechnolgy)
[24] Multivalent avimer proteins evolved by exon shuffling of a family of
human receptor domains
DOI: 10.1038/nbt1166
[25] Artificial cell-cell communication in yeast Saccharomyces cerevisiae
using signaling elements from Arabidopsis thaliana
DOI: 10.1038/nbt1162
NATURE GENETICS (<http://www.nature.com/naturegenetics>)
[26] A genome-wide RNA interference screen in Drosophila melanogaster cells
for new components of the Hh signaling pathway
DOI: 10.1038/ng1682
[27] Deficiency of UBR1, a ubiquitin ligase of the N-end rule pathway,
causes pancreatic dysfunction, malformations and mental retardation
(Johanson-Blizzard syndrome)
DOI: 10.1038/ng1681
[28] Adaptive evolution of bacterial metabolic networks by horizontal gene
transfer
DOI: 10.1038/ng1686
Nature STRUCTURAL & MOLECULAR BIOLOGY
(<http://www.nature.com/natstructmolbiol>)
[29] A conserved processing mechanism regulates the activity of
transcription factors Cubitus interruptus and NF-kappaB
DOI: 10.1038/nsmb1018
[30] A miniature yeast telomerase RNA functions in vivo and reconstitutes
activity in vitro
DOI: 10.1038/nsmb1019
[31] Concerted regulation of nuclear and cytoplasmic activities of SR
proteins by AKT
DOI: 10.1038/nsmb1020
[32] Folding zone inside the ribosomal exit tunnel
DOI: 10.1038/nsmb1021
[33] Structure and chromosomal DNA binding of the SWIRM domain
DOI: 10.1038/nsmb1022
[34] Swc2 is a widely conserved H2AZ-binding module essential for
ATP-dependent histone exchange
DOI: 10.1038/nsmb1023
[35] RNA-mediated interaction between the peptide-binding and GTPase domains
of the signal recognition particle
DOI: 10.1038/nsmb1025
[36] Insights into voltage-gated calcium channel regulation from the
structure of the Cav1.2 IQ domain-Ca2+/calmodulin complex
DOI: 10.1038/nsmb1027
******************************************************************
PAPER FOR IMMEDIATE RELEASE FROM Nature STRUCTURAL & MOLECULAR BIOLOGY
(<http://www.nature.com/natstructmolbiol>)
[37] The Cbf5-Nop10 complex is a molecular bracket that organizes box H/ACA
RNPs
DOI: 10.1038/nsmb1036
****************************************************************************
GEOGRAPHICAL LISTING OF AUTHORS
The following list of places refers to the whereabouts of authors on the
papers numbered in this release. The listing may be for an author's main
affiliation, or for a place where they are working temporarily. Please see
the PDF of the paper for full details.
ARGENTINA
Buenos Aires: 32
AUSTRIA
Vienna: 28
BELGIUM
Brussels: 13
BRAZIL
Sao Paolo: 28
CANADA
Toronto: 2, 28
CHINA
Kunming: 20
Shanghai: 5
COSTA RICA
San Jose: 28
CROATIA
Zagreb: 28
FRANCE
Bordeaux: 19
Clermont-Ferrand: 28
Paris: 15
Strasbourg: 20
Toulouse: 4
GERMANY
Aachen: 28
Berlin: 4
Bremen: 1
Erlangen: 28
Griefswald: 28
Heidelberg: 29
Marburg: 11
Martinsried near Munich: 1
Muenster: 28
HUNGARY
Budapest: 29
ISRAEL
Afula: 28
Haifa: 28
JAPAN
Kagoshima: 12
Kobe: 11
Otsu: 17
Tokyo: 3, 8, 17
Wako: 12
THE NETHERLANDS
Nijmegen: 28
Utrecht: 28
SPAIN
Barcelona: 13
UNITED KINGDOM
Bath: 29
Cambridge: 7
Edinburgh: 32
Manchester: 29
Oxford: 5, 11, 23
UNITED STATES OF AMERICA
Arizona
Tempe: 7
California
Berkeley: 16, 18, 36
Duarte: 24
Los Angeles: 17
Mountain View: 25
Pasadena: 28
San Francisco: 2, 18, 23, 37
Stanford: 10, 18
Colorado
Boulder: 31
Florida
Tampa: 24
Illinois
Chicago: 23, 30
Evanston: 15, 30
Iowa
Iowa City: 9
Louisiana
New Orleans: 14, 19
Maryland
Baltimore: 17, 23, 24
Bethesda: 19, 23, 35
Charlestown: 23
Frederick: 23
Massachusetts
Boston: 2, 9, 27
Cambridge: 9, 27
Waltham: 2
New Jersey
Princeton: 26
New York
New York: 9, 22, 23, 34
Pennsylvania
Philadelphia: 9, 21, 22, 33
Pittsburgh: 28
Rhode Island
Providence: 6
Texas
Houston: 23
Smithville: 2
Virginia
Charlottesville: 19
Washington
Seattle: 38
PRESS CONTACTS...
For media inquiries relating to embargo policy for all the Nature Research
Journals:
Katharine Mansell (Nature London)
Tel: +44 20 7843 4658; E-mail: [email protected]
For media inquiries relating to editorial content/policy for the Nature
Research Journals, please contact the journals individually:
Nature Biotechnology (New York)
Kathy Aschheim
Tel: +1 212 726 9346; E-mail: [email protected]
Nature Cell Biology (London)
Bernd Pulverer
Tel: +44 20 7843 4892; E-mail: [email protected]
Nature Chemical Biology (Boston)
Beatrice Chrystall
Tel: +1 617 475 9241, E-mail: [email protected]
Nature Genetics (New York)
Orli Bahcall
Tel: +1 212 726 9311; E-mail: [email protected]
Nature Immunology (New York)
Laurie Dempsey
Tel: +1 212 726 9372; E-mail: [email protected]
Nature Materials (London)
Maria Bellantone
Tel: +44 20 7843 4556; E-mail: [email protected]
Nature Medicine (New York)
Juan Carlos Lopez
Tel: +1 212 726 9325; E-mail: [email protected]
Nature Neuroscience (New York)
Sandra Aamodt (based in California)
Tel: +1 530 795 3256; E-mail: [email protected]
Nature Structural & Molecular Biology (New York)
Ed Feng
Tel: +1 212 726 9351; E-mail: [email protected]
Nature Publishing Group (NPG) is a division of Macmillan Publishers Ltd,
dedicated to serving the academic and professional scientific community.
NPG's flagship title, Nature, is the world's most highly-cited weekly
multidisciplinary journal and was first published in 1869. Other
publications include Nature research journals, Nature Reviews, Nature
Clinical Practice, and a range of prestigious academic journals, including
society-owned publications.
NPG is a global company, with headquarters in London and offices in New
York, San Francisco, Washington DC, Boston, Tokyo, Paris, Munich and
Basingstoke. For more information, please go to www.nature.com
