Frank Lab

Welcome to the Frank Lab

We investigate the mechanism of translation on the ribosome by using cryo-electron microscopy and single-particle reconstruction.

Recent Publications

Book: Molecular Machines in Biology: Workshop of the Cell
Publisher: Cambridge University Press
Author: Joachim Frank
Click here to order.
[Description]

Article: High-resolution cryo-electron microscopy structure of the
Trypanosoma brucei ribosome
Journal: Nature
Author: Yaser Hashem, et al.
[Abstract]

Ribosomes, the protein factories of living cells, translate genetic information carried by messenger RNAs into proteins, and are thus involved in virtually all aspects of cellular development and maintenance. The few available structures of the eukaryotic ribosome reveal that it is more complex than its prokaryotic counterpart, owing mainly to the presence of eukaryote-specific ribosomal proteins and additional ribosomal RNA insertions, called expansion segments. The structures also differ among species, partly in the size and arrangement of these expansion segments. Such differences are extreme in kinetoplastids. Here we present a high-resolution (~5Å) cryo-electron microscopy structure of the ribosome of Trypanosoma brucei, the parasite that is transmitted by the tsetse fly and that causes African Sleeping Sickness. The atomic model reveals the unique features of this ribosome, characterized mainly by the presence of unusually large eukaryotic expansion segments and ribosomal protein extensions leading to the formation of four additional inter-subunit bridges. We also find additional rRNA insertions, including one large rRNA domain that is not found in other eukaryotes. Furthermore, the structure reveals the five cleavage sites of the kinetoplastid large ribosomal subunit rRNA chain, which is known to be cleaved uniquely into six pieces, and suggests that the cleavage is important for the maintenance of the T. brucei ribosome in the observed structure. We discuss several possible implications of the large rRNA expansion segments for the translation regulation process, and we show a possible link between the protein translation initiation process and expansion segments 6 and 7 on the small ribosomal subunit. Our structure could serve as a basis for future experiments aimed at understanding the functional importance of these kinetoplastid-specific ribosomal features in protein translation regulation, an essential step towards finding effective and safe kinetoplastid-specific drugs.

Article: High-resolution cryo-electron microscopy structure of the
Trypanosoma brucei ribosome.
Journal: Albany 2013: Book of Abstracts
Author: Yaser Hashem, et al.
[Abstract]

Ribosomes, the protein factories of living cells, translate genetic information carried by messenger RNAs into proteins, and are thus involved in virtually all aspects of cellular development and maintenance. The few available structures of the eukaryotic ribosome reveal that it is more complex than its prokaryotic counterpart, owing mainly to the presence of eukaryote-specific ribosomal proteins and additional ribosomal RNA insertions, called expansion segments. The structures also differ among species, partly in the size and arrangement of these expansion segments. Such differences are extreme in kinetoplastids. Here we present a high-resolution (~5Å) cryo-electron microscopy structure of the ribosome of Trypanosoma brucei, the parasite that is transmitted by the tsetse fly and that causes African Sleeping Sickness. The atomic model reveals the unique features of this ribosome, characterized mainly by the presence of unusually large eukaryotic expansion segments and ribosomal protein extensions leading to the formation of four additional inter-subunit bridges. We also find additional rRNA insertions, including one large rRNA domain that is not found in other eukaryotes. Furthermore, the structure reveals the five cleavage sites of the kinetoplastid large ribosomal subunit rRNA chain, which is known to be cleaved uniquely into six pieces, and suggests that the cleavage is important for the maintenance of the T. brucei ribosome in the observed structure. We discuss several possible implications of the large rRNA expansion segments for the translation regulation process, and we show a possible link between the protein translation initiation process and expansion segments 6 and 7 on the small ribosomal subunit. Our structure could serve as a basis for future experiments aimed at understanding the functional importance of these kinetoplastid-specific ribosomal features in protein translation regulation, an essential step towards finding effective and safe kinetoplastid-specific drugs.

Article: Mechanism of tetracycline resistance by ribosomal protection
protein Tet(O).
Journal: Nature Communications
Author: Wen Li, et al.
[Abstract]

Article: Affinity grid-based cryo-EM of PKC binding to RACK1 on the ribosome.
Journal: Journal of Structural Biology
Author: G. Sharma, J. Pallesen, S. Das, R. Grassucci, R. Langlois, C.M. Hampton, D.F. Kelly, A. des Georges, and J. Frank
[Abstract]

Recent Blog

Dr. Frank asked to join Faculty of 1000

May 7, 2013

Dr. Frank is now a member of the Faculty of 1000. F1000 identifies and recommends important articles in biology and medical research publications. Articles are selected by a peer-nominated global 'Faculty' of the world's leading scientists and clinicians who then rate them and explain their importance. From the numerical ratings awarded, F1000 has created a unique system for quantifying the importance of individual articles. Launched in 2002, F1000 was conceived as a collaboration of 1,000 international Faculty Members. The name stuck even...

Welcome to the Frank Lab

Recent Publications

Recent Blog

Dr. Frank asked to join Faculty of 1000

Paper accepted by eLife

Papers accepted by Cell and Biopolymers

Papers accepted by Nature and JSB

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