The translating ribosome: towards mature proteins

The structure and function of the ribosome was conceptually revealed during the past 10 years, and in 2009 V. Ramakrishnan, T. A. Steitz and A. E. Yonath were awarded the Nobel Prize in Chemistry for their seminal contributions to this field including high-resolution structures of the prokaryotic complexes, the largest functional complex ever studied. The 3D structure of plastid and mitochondrial ribosomes was also revealed during the same decade. In 2010, several major studies have reported high-resolution structures of the eukaryotic cytosolic ribosome (yeast and plant), completing the full picture. Translation requires intricate communication between multiple components to achieve speed, accuracy, and regulation. Detailed understanding of the mechanism of protein synthesis is now progressively appearing in the literature. It includes the steps of initiation, elongation and terminations and involves the interactions with various translation factors and tRNAs. Communication between translation factors, the ribosome, tRNA, mRNA, and other cellular pathways is the mechanistic basis for the high levels of control that exist in translation. Concomitant to these major advances, new approaches have made a marked impact on the relevance of non-ribosomal proteins that permanently or transiently associate with the ribosome. In this new era where the mysteries of the ribosome now appear to be much more tractable, the time has come to shed light on selected points of the mode of function of the ribosome. In the post-genomic-era, it has become evident that further steps after protein synthesis, namely the folding and processing of proteins, ultimately determine the functional biomolecule. Once the nascent polypeptide emerges from the ribosome, it is immediately challenged by a number of cellular factors (chaperones, modifying enzymes etc.) that will determine the fate of the protein even before it has been fully made. In addition, cotranslational events such as eukaryotic translation initiation, processing and folding are tightly regulated by a number of cellular pathways responsible for cellular growth, proliferation, viral infection and apoptosis.

The current conference aims at linking the processes occurring on the ribosome, namely mRNA decoding, protein synthesis (translation) and co-translational processing, and even shedding light on the downstream implications on protein function. The ambition is to bridge two interdependent fields, one now well-established (the ribosome progressing on the way to translation) and the second which is just emerging (the fate of nascent peptides) and get new insight on the dynamicity of the process and the interconnections between the two processes.
+ show speakers and program
ARNESEN Thomas (Bergen, Norway)
Protein N-terminal transferases and N-terminal acetylation

BAN Nenad (Zürich, Switzerland)
The complete atomic structure of the eukaryotic 40S ribosomal subunit and implications for the process of translation initiation

BAUMEISTER Wolfgang (Martinsried, Germany)
Higher order structures of ribosomes revealed by electron tomography

BECKMANN Roland (München, Germany)
Cryo-EM studies on ribosomal stalling and recycling

BUKAU Bernd (Heidelberg, Germany)
Interplay of ribosome-associated factors mediating the processing and folding of nascent polypeptides

CAVAGNERO Silvia (Madison, USA)
Watching protein folding at the exit tunnel

DEUERLING Elke (Konstanz, Germany)
Functional versatility of ribosome-associated chaperones in protein folding and translational control

EHRENBERG Måns (Uppsale, Sweden)
Efficiency-accuracy trade-off lines in genetic code translation

GEVAERT Kris (Gent, Belgium)
N-terminomics technologies for studying (the degree of) protein alpha-N-acetylation

GIGLIONE Carmela (Gif sur Yvette, France)
Dynamicity of N-terminal cotranslational modifications

GILLET Reynald (Rennes, France)
Lost in translation: tmRNA-SmpB to the rescue

HEGDE Ramanujan (Bethesda, USA)
Chaperoning membrane proteins from the ribosome to their destination

IGNATOVA Zoya (Martinsried, Germany)
Pausing translational elongation to fine-tune protein biogenesis

KLAHOLZ Bruno (Illkirch, France)
The translating ribosome visualized by multi-scale structural analysis

POOL Martin (Manchester, United Kingdom)
Interplay between N-terminal processing and protein targeting of nascent polypeptides

PUGLISI Jody (Stanford, USA)
Title to be coming

RAMAKRISHNAN Venki (Cambridge, United Kingdom)
Crystallography of functional states of the ribosome

ROMBY Pascale (Strasbourg, France)
Translation initiation of structured and regulated mRNAs in bacteria

ROSPERT Sabine (Freiburg, Germany)
Function of eukaryotic protein biogenesis factors at the exit of the ribosomal tunnel

SARGUEIL Bruno (Paris, France)
Loading the ribosome onto the mRNA, the intriguing case of HIV

STEITZ Thomas (New Haven, USA)
Structures of complexes of the 70S ribosome with factors and antibiotics

VARSHAVSKY Alexander (Pasadena, USA)
Recent discoveries about the N-End rule pathway

YONATH Ada (Rehovot, Israel)
From the genetic code to folded proteins

YOSHIZAWA Satoko (Gif sur Yvette, France)
Nanotechnologies for translational studies and applications

YUSUPOV Marat (Illkirch, France)
Structure of the eukaryotic ribosome at 3.0Å resolution

2 Jun - 6 Jun 2012
meeting website