Summary report of the Caribbean meeting of experts on Implementation of the SIDS Plan of Action

The Caribbean Meeting of Experts on Implementation of the SIDS Programme of Action, held at the Holiday Inn Hotel, Port of Spain, Trinidad and Tobago, 17-19 May 1995 was convened to review progress towards implementation of the SIDS Programme of Action (SIDS-POA), to discuss constraints on the effective implementation of the Programme and to agree on priority areas for action. It was organized by the Economic Commission for Latin America and the Caribbean/Caribbean Development and Cooperation Committee (ECLAC/CDCC), in collaboration with the United Nations Development Programme’s Special Unit for Technical Cooperation among Developing Countries (UNDP/TCDC), the United Nations Environment Programme (UNEP), the University of the West Indies Centre for Environment and Development (UWICED), and the Caribbean Community (CARICOM). A copy of the programme and a list of documents are attached to this report as Annex I and II respectively.

Performance of Latin America and the Caribbean during the first years of the Decade of Action for Road Safety

This issue of the FAL Bulletin examines the performance of the countries of Latin America and the Caribbean during the first years of the decade of action for road safety. This document is part of the activities being undertaken by ECLAC as a United Nations regional commission in preparation for the Second Global High-Level Conference on Road Safety, which is to take place in Brasilia on 18 and 19 November 2015.

Purification and structural characterization of snake venom proteins

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Influence of abutment-to-fixture design on reliability and failure mode of all-ceramic crown systems

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Comprehensive Analysis of Gene Expression Profiles of the Beet Armyworm Spodoptera exigua Larvae Challenged with Bacillus thuringiensis Vip3Aa Toxin

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Mechanisms of action of fluoridated acidic liquid dentifrices against dental caries

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Combining Experimental Evidence and Molecular Dynamic Simulations To Understand the Mechanism of Action of the Antimicrobial Octapeptide Jelleine-I

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Natural compounds isolated from Brazilian plants are potent inhibitors of hepatitis C virus replication in vitro

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Production of active recombinant eIF5A: reconstitution in E. coli of eukaryotic hypusine modification of eIF5A by its coexpression with modifying enzymes

Eukaryotic translation initiation factor 5A (eIF5A) is the only cellular protein that contains the polyamine-modified lysine, hypusine [Nε-(4-amino-2-hydroxybutyl)lysine]. Hypusine occurs only in eukaryotes and certain archaea, but not in eubacteria. It is formed post-translationally by two consecutive enzymatic reactions catalyzed by deoxyhypusine synthase (DHS) and deoxyhypusine hydroxylase (DOHH). Hypusine modification is essential for the activity of eIF5A and for eukaryotic cell proliferation. eIF5A binds to the ribosome and stimulates translation in a hypusine-dependent manner, but its mode of action in translation is not well understood. Since quantities of highly pure hypusine-modified eIF5A is desired for structural studies as well as for determination of its binding sites on the ribosome, we have used a polycistronic vector, pST39, to express eIF5A alone, or to co-express human eIF5A-1 with DHS or with both DHS and DOHH in Escherichia coli cells, to engineer recombinant proteins, unmodified eIF5A, deoxyhypusine- or hypusine-modified eIF5A. We have accomplished production of three different forms of recombinant eIF5A in high quantity and purity. The recombinant hypusine-modified eIF5A was as active in methionyl-puromycin synthesis as the native, eIF5A (hypusine form) purified from mammalian tissue. The recombinant eIF5A proteins will be useful tools in future structure/function and the mechanism studies in translation.