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Special Symposia View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by MPG.PuRe Abstracts N1 – IUBMB 50th Anniversary Symposium: Protein Structure and Function N1-001 receptor tyrosine phosphatases and also organizes the actin cyto- Molecular biology of mammalian prions skeleton. Our studies aim to compare the activities of IRSp53 and A. Aguzzi MIM, using known structural information to create mutants and Department of Pathology, Institute of Neuropathology, University dissect the functions of these proteins in signalling to cell motility. Conclusions: IRSp53 and MIM contain conserved actin bund- Hospital Zurich, Zu¨rich, – Switzerland. E-mail: [email protected] ling domains and are thus effectors as well as scaffold proteins. Both proteins bundle actin filaments by a conserved mechanism Transmissible spongiform encephalopathies (TSE) are fatal neuro- and this is important for their function in mammalian cells. degenerative diseases of humans and animals. The underlying infectious agent, the prion, accumulates not only in the central ner- vous system (CNS) but also in secondary lymphoid organs. I will N1-003 revisit the role of the immune system in peripheral prion pathogen- Structural proteomics of transcription and esis, while focusing on the mechanisms by which extraneural and translation proteins extralymphatic prion infectivity develops. Interestingly, the same S. Yokoyama1,2 pro-inflammatory cytokines and homeostatic chemokines that are 1RIKEN Genomic Sciences Center, RIKEN Harima Institute at involved in lymphoid neogenesis and compartmentalization of SPring-8, Yokohama, Japan, 2Department of Biophysics and immune cells appear to represent the crucial molecular switches Biochemistry, Graduate School of Science, University of Tokyo, responsible for the establishment of extraneural prion reservoirs. Tokyo, Japan. E-mail: [email protected] We have been studying structural and functional aspects of var- N1-002 ious transcription and translation proteins, such as RNA polym- Regulation of the actin cytoskeleton by IRSp53 erases, transcriptional regulators, RNA helicases, RNA and MIM proteins processing and modifications enzymes, aminoacyl-tRNA synthe- tases, and translation factors, mainly by X-ray crystallography, L. M. Machesky, T. H. Millard, G. Bompard, S. J. Sharp, as a part of the national project of structural proteomics. The J. A. Woodings and K. Futterer crystal structure of the bromodomain of human Brd2, as well as School of Biosciences, University of Birmingham, Birmingham, those of its complexes with different peptides corresponding to UK. E-mail: [email protected] the acetylated histone H4 reveals many surprising features inclu- The mechanism of actin cytoskeletal reorganization by Rho family ding the recognition of the site-specific acetylation pattern of the small GTPases is complex and involves multiple protein interac- lysine residues (the ‘‘histone code’’) in epigenetic transcriptonal tions. We recently solved the crystal structure of the IRSp53- regulation. We have determined the crystal structure of the heli- MIM actin bundling domain (IMD) of the human IRSp53. case fragment of Vasa bound with a single-stranded RNA and IRSp53 binds to the small GTPases Rac and Cdc42 and is an ATP analogue. The observations illustrate the nucleic acid involved in the assembly of both filopodia and lamellipodia in translocation, coupled to ATP hydrolysis, by the ‘‘inchworm’’ mammalian cells. It is thought to act as a scaffold, assembling mechanism of the helicase superfamily II, to which the DEAD- complexes of actin regulatory proteins (such as Scar/WAVE, box family belongs. Mechanisms of tRNA and amino acid recog- Mena/VASP) near the plasma membrane. We also found that it is nition by aminoacyl-tRNA synthetases have been studied on the an effector, inducing actin bundling directly through the IMD. basis of their crystal structures and mutagenesis. For strict selec- The related protein, Missing in Metastasis (MIM) interacts with tion of amino acids, many synthetases have the ‘‘editing 4 Abstracts domain’’. The crystal structures of a complex of archaeal leucyl- oms has been described and resulted in important discoveries. tRNA synthetase and a leucine tRNA demonstrate how the 3’- The aim of the present study was to isolate the toxin from Tityus terminus of tRNA is relocated from the aminoacylation domain serrulatus venom (TsV) with action on the CS and to evaluate its to the editing domain. effects using in vitro assays. Methods: The toxin was purified from TsV by ion exchange chromatography on CM-cellulose-52 followed by reverse phase N1-004 HPLC (C-4) of lyophilized fraction I. Complement consumption Signaling via GTP-binding proteins of the Ras by the toxin was evaluated using in vitro haemolytic assays, im- superfamily munoelectrophoresis and two-dimension immunoelectrophoresis of complement components (factor B and C3). A. Wittinghofer Results: The isolated toxin is a single polypeptide chain showing Structural Biology, Max-Planck-Institute for molecular Physiol- a single band in SDS-PAGE, corresponding to an approximate ogy, Dortmund, Germany. Mr of 10 000. This protein induced a concentration-dependent E-mail: [email protected] reduction in haemolytic activity of the classical/lectin (CP) and Guanine nucleotide binding proteins (GNBPs) cycle between a alternative (AP) complement pathways, with an IC50 (sample GDP-bound inactive and a GTP-bound active state. The switch- concentration inhibiting 50% of the lytic activity) of 22.08 and ON reaction involves the exchange of tightly bound GDP against 62.66 mg for CP and AP, respectively. Alterations in C3 and fac- GTP, while the switch-OFF mechanism involves the enzymatic tor B electrophoretic mobility after incubation of normal human cleavage of GTP to GDP. The first reaction is catalyzed by guan- serum with toxin (45 mg), were identical to those obtained with ine nucleotide exchange factors GEFs, while the second is activa- zymosan (positive control). ted by GTPase-activating proteins GAPs. The inability of certain Conclusion: Our results show that the toxin is able to activate of these proteins to be down regulated leads to various forms of the complement system leading to reduction of serum lytic activ- cancer. The biological function of the GTP-binding proteins relies ity and Factor B and C3 cleavage. Therefore, this toxin may play on the ability to switch between two different conformations, only an important role in the inflammatory response observed upon one of which has a high affinity to the downstream target. The scorpion envenomation. common structural principles of the switch mechanism will be Acknowledgments: This work was financially supported by presented, and examples for how Ras and Rho proteins in their FAPESP and CNPq. active GTP-bound form recognize downstream targets will be dis- cussed, together with the biological consequences. N1-007P Interactions of HIV-1 integrase with modified analogs of viral DNA: implications for N1-005 understanding integration mechanism 50 Years of IUB(MB) J. Agapkina, M. Smolov and M. Gottikh W. J. Whelan Nucleic Acid Chemistry lab., Chemical dep., Belozersky Institut of Biochemistry, University of Miami, Miami, FL, USA. Physico-Chemical Biology, Moscow State University, Moscow, E-mail: [email protected] Russian Federation. E-mail: [email protected] This will be an account of the history of the International Union Human immunodeficiency virus type 1 (HIV-1) is related to the of Biochemistry and Molecular Biology (IUBMB), which began class of retroviruses, which genome consists from RNA molecules. life as the IUB, from its admission as a Union into the Interna- After RNA reverse transcription, a DNA copy of the viral RNA tional Council of Scientific Unions (ICSU), in 1955, the occasion is integrated into genome of an infected cell. The viral DNA integ- for this 50th anniversary celebration, but also mentioning the ration is one of the most important steps of the whole retroviral way in which idea to form a Union was conceived and implemen- replication cycle, and it is effectuated by a viral enzyme, integrase ted, beginning at the first International Congress of Biochemistry, (IN). It is known that IN recognizes specific sequences localized at held in Cambridge in 1949. The speaker was the first Secretary viral DNA U3 and U5 LTRs, binds them and catalyzes two nuc- General of FEBS (1965–1967), the General Secretary of IUB leotide removal reaction from 3’-ends of each strand. It is the first (1973–1983) and President of IUBMB (1997–2000). He will offer integration stage that is named 3’-end processing. Later IN medi- prognostications for the next 50 years. ates strand transfer reaction consisting in processed virus DNA embedding into the host DNA. In order to reveal what structural features of the viral DNA mostly determine the sequence-specifici- N1-006P ty of its recognition and processing by IN, in the current work we Isolation of a new toxin from Tityus serrulatus studied systematically how the double helix structure of viral scorpion venom with action on the DNA influences on the HIV-1 integrase activity in 3’-end process- complement system ing reaction. For this purpose we synthesized a set of modified DNA duplexes, which sequence mimicked U5 LTR of the viral D. T. Bertazzi1, A. I. d. Assis-Pandochi1, A. E.-C.-S. Azzolini1, DNA. Nucleosides at different positions of processed and/or non- S. V. Sampaio2 and E. C. Arantes1 processed strands were consistently replaced by a non-nucleoside 1Departamento de Fı´sica e Quı´mica, Universidade de Sa˜o Paulo, insertion, 1,3-propanediol residue, or nucleosides containing Faculdade de Cieˆncias Farmaceˆuticas de Ribeira˜o Preto, Ribeira˜o modified sugar residues: 2’-aminonucleosides and 2’-O-methylnu- Preto, Sa˜o Paulo Brazil, 2Departamento de Ana´lises Clı´nicas, Tox- cleosides. We concentrated our attention on the study of the integ- icolo´gicas e Bromatolo´gicas, Universidade de Sa˜o Paulo, Faculdade rase intetaction with viral DNA third adenosine situated close to de Cieˆncias Farmaceˆuticas de Ribeira˜o Preto, Ribeira˜o Preto, Sa˜o the 3’-processing point.
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