Research Area C - Publications 2013

ACS Chem. Biol., 2013, DOI: 10.1021/cb400723j, 9 (2), pp 347–352 published on 03.12.2013
ACS Chem. Biol., online article
sattler_acschembio2014_500.100x0.jpg

Many cellular processes are regulated by posttranslational modifications that are recognized by specific domains in protein binding partners. These interactions are often weak, thus allowing a highly dynamic and combinatorial regulatory network of protein–protein interactions. We report an efficient strategy that overcomes challenges in structural analysis of ...

|READ MORE|

Cell, 2013, http://dx.doi.org/10.1016/j.cell.2013.10.024, Volume 155, Issue 5, Pages 1075–1087 published on 21.11.2013
Cell, online article
cramer_cell2013_500.100x0.jpg

Pervasive transcription of eukaryotic genomes stems to a large extent from bidirectional promoters that synthesize mRNA and divergent noncoding RNA (ncRNA). Here, we show that ncRNA transcription in the yeast S. cerevisiae is globally restricted by early termination that relies on the essential RNA-binding factor Nrd1. Depletion of Nrd1 from the nucleus results ...

|READ MORE|

PLOS, Volume 9, Issue 11, e1003914, doi:10.1371/journal.pgen.1003914

PLOS, online article

cramer_plos2013_no28_500.100x0.jpg

Messenger RNA (mRNA) synthesis and export are tightly linked, but the molecular mechanisms of this coupling are largely unknown. In Saccharomyces cerevisiae, the conserved TREX complex couples transcription to mRNA export and mediates mRNP formation. Here, we show that TREX is recruited to the transcription machinery by direct interaction of its subcomplex THO ...

|READ MORE|

The Journal of Biological Chemistry, 2013, doi: 10.1074/jbc.M113.499707, 289, 437-448. published on 14.11.2013
The Journal of Biological Chemistry, online article
sattler_etal_jbc2014_500.100x0.jpg

Protein import into peroxisomes relies on the import receptor Pex5, which recognizes proteins with a peroxisomal targeting signal 1 (PTS1) in the cytosol and directs them to a docking complex at the peroxisomal membrane. Receptor-cargo docking occurs at the membrane-associated protein Pex14. In human cells, this interaction is mediated by seven conserved ...

|READ MORE|

JBC, 2013, doi: 10.1074/jbc.M113.508267, published on 06.11.2013
JBC, online article
cramer_jbiolchem2013_500.100x0.jpg

The RNA polymerase II (RNApII) C-terminal domain (CTD)-interacting domain (CID) proteins are involved in two distinct RNApII termination pathways and recognize different phosphorylated forms of CTD. To investigate the role of differential CTD-CID interactions in the choice of termination pathway, we altered the CTD-binding specificity of Nrd1 by domain swapping. ...

|READ MORE|

American Society for Microbiology, 2013, doi: 10.1128/AAC.01994-13, vol. 58 no. 1 472-480 published on 04.11.2013
American Society for Microbiology, online article
wilson_aac2013_500.100x0.jpg

Ketolides, the third generation of expanded-spectrum macrolides, have in the last years become a successful weapon in the endless war against macrolide-resistant pathogens. Ketolides are semisynthetic derivatives of the naturally produced macrolide erythromycin, displaying not only improved activity against some erythromycin-resistant strains but also increased ...

|READ MORE|

Nature, 2013, doi:10.1038/nature12712, 502, 650–655 published on 23.10.2013
Nature, online article
cramer_nature2013_5001.100x0.jpg

Transcription of ribosomal RNA by RNA polymerase (Pol) I initiates ribosome biogenesis and regulates eukaryotic cell growth. The crystal structure of Pol I from the yeast Saccharomyces cerevisiae at 2.8 Å resolution reveals all 14 subunits of the 590-kilodalton enzyme, and shows differences to Pol II. An ‘expander’ element occupies the DNA template site and ...

|READ MORE|

Molecular and Cellular Biology, 2013, doi: 10.1128/MCB.00361-13, vol. 33, no.19, 3805-3816, published on 22.10.2013
Molecular and Cellular Biology, online article
cramer_molcell_biol_2013_lidschreiber_3805_16_500.100x0.jpg

After transcription initiation, RNA polymerase (Pol) II escapes from the promoter and recruits elongation factors. The molecular basis for the initiation-elongation factor exchange during this transition remains poorly understood. Here, we used chromatin immunoprecipitation (ChIP) to elucidate the initiation-elongation transition of Pol II in the budding yeast ...

|READ MORE|

Advanced Functional Materials, 2013, DOI: 10.1002/adfm.201302411, published on 16.10.2013
Advanced Functional Materials, online article
kessler_707_2013_afmjournal_500.100x0.jpg

The interaction of specific surface receptors of the integrin family with different extracellular matrix-based ligands is of utmost importance for the cellular adhesion process. A ligand consists of an integrin-binding group, here cyclic RGDfX, a spacer molecule that lifts the integrin-binding group from the surface and a surface anchoring group. c(-RGDfX-) ...

|READ MORE|

Expert Opin., 2013, doi:10.1517/13543776.2013.818133, Vol. 23, No. 10 , Pages 1273-1295 published on 15.10.2013
Expert Opin., online article
kessler_705_2013_500.100x0.jpg

Integrins are heterodimeric cell surface receptors, which enable adhesion, proliferation, and migration of cells by recognizing binding motifs in extracellular matrix (ECM) proteins. As transmembrane linkers between the cytoskeleton and the ECM, they are able to recruit a huge variety of proteins and to influence signaling pathways bidirectionally, thereby ...

|READ MORE|

Molecular Cell, 2013, http://dx.doi.org/10.1016/j.molcel.2013.09.010, Volume 52, Issue 1, Pages 52–62 published on 10.10.2013
Molecular Cell, online article
cramer_molcell_okt2013_500.100x0.jpg

The rates of mRNA synthesis and degradation determine cellular mRNA levels and can be monitored by comparative dynamic transcriptome analysis (cDTA) that uses nonperturbing metabolic RNA labeling. Here we present cDTA data for 46 yeast strains lacking genes involved in mRNA degradation and metabolism. In these strains, changes in mRNA degradation rates are ...

|READ MORE|

Nature Structural & Molecular Biology, 2013, doi:10.1038/nsmb.2683, 20, 1298–1303 published on 06.10.2013
Nature Structural & Molecular Biology, online article
cramer_nsmb2013_500.100x0.jpg

Here we report the crystal structure of the human mitochondrial RNA polymerase (mtRNAP) transcription elongation complex, determined at 2.65-Å resolution. The structure reveals a 9-bp hybrid formed between the DNA template and the RNA transcript and one turn of DNA both upstream and downstream of the hybrid. Comparisons with the distantly related RNA polymerase ...

|READ MORE|

CIPSM Movie
LMUexcellent
TU München
MPG
Helmholtz München
MPI of Neurobiology
MPI of Biochemistry