Guidelines for Abstract Submission


  1. The submission of abstracts is only possible after registration.
  2. The author/presenter of the paper must be registered for the Congress.
  3. An author may register and present only ONE abstract; however, they may co-author others.
  4. Only abstracts of unpublished papers may be submitted.
  5. Project descriptions, paper intentions and published papers will not be accepted.
  6. The abstract must be sent electronically, DOC/DOCX format, only. Works in PDF format will not be accepted.
  7. The abstract must be written in English.
  8. The submitted abstracts will be analyzed by the Congress Scientific Committee and the result will be made available on the event website by participant’s name or CPF number.
  9. The analysis encompasses the following aspects: relevant, clearly stated objectives; appropriate methodology; clearly presented results; pertinent conclusions. The text quality (grammar, spelling and typing) is the author’s responsibility and is one of the Scientific Committee’s evaluation criteria.
  10. After Jun 26th, the abstract submission forms for oral presentation and poster presentations will be unavailable.
  11. The abstracts selected for the poster presentation should be displayed at the Poster Session, in English, during the event. The designated area for each poster will be a 1m x 1m. panel.
  12. The Poster must have a hanging cord and/or adhesive tape to be held in place.



The Abstracts submitted to BBEST may be selected for Oral presentations during BBEST or may be presented as Poster. The Scientific Program Committee will select Abstracts for Oral presentations and the authors will be informed about the form of presentation through the BBEST website. The authors must indicate their preferred form of presentation (Oral or Poster) during the registration and abstract submission procedures.



  1. Biomass, agronomy, breeding, biotechnological aspects of plant feedstock;
  2. Biofuel Technologies, including biomass process engineering and biofuels production;
  3. Alcoholchemistry, Sugarchemistry, Oil Chemistry, Biorefineries, Bio-based chemicals, and Biomaterials;
  4. Engines and other conversion devices including aviation aplications;
  5. Sustainability and Impacts.



The number of words (from introduction to conclusion) must be between 200 and 450 in either MS-Word program files (.doc or .docx).


Abstract Example

Dual targeting of RNA-binding proteins to mitochondria and chloroplasts

Morgante, CV1,2; Otto, PA3; Silva-Filho, MC1; Gualberto, JM2,3.

1Escola Superior de Agricultura Luiz de Queiroz, USP, São Paulo, SP
2Centre Nacional de La RechercheScientifique (CNRS), Estrasburgo, França
3Instituto de Biociências, USP, São Paulo, SP

Keywords: Arabidopsis, GFP, point mutations

A massive transfer of mitochondria and chloroplast DNA to the cell nucleus occurred during the evolution of these organelles. As a consequence, most of their proteins are encoded by nuclear genes and have specific N-terminal targeting sequences. Although cell compartmentalization enables distinct roles to organelles, they may have overlapping functions, and a given protein may be required to more than one compartment. Dual targeting appears as a strategy to deal with this requirement. Approximately 30 Arabidopsis thaliana proteins are known to be dual targeted, and most of them are involved in transcription, translation, and oxidative metabolism. Herein we describe the dual targeting of three RNA-binding proteins of A. thaliana to mitochondria and chloroplasts. These proteins are characterized by a conserved RNA recognition motif (RRM) and a C-terminal glycine-rich sequence. Proteins containing a RRM motif are involved in post-transcriptional processes and regulation of gene expression. Using a GFP approach and bombardment of Nicotiana benthamiana mesophyl cells, we demonstrated the dual targeting of the RBP1a (At4g13850), RBP1b (At3g23830), and RPS19 (At5g47320) proteins. Their N-terminal amino acid sequences are relatively conserved, suggesting that they originated by gene duplication after acquisition of the targeting sequence (TS). When the first 39 amino acids of RBP1b were deleted, the protein was localized only to the cytosol, indicating that the signal for RBP1b targeting is located in its N-terminal region. In order to identify residues important for chloroplast and/or mitochondria targeting, we introduced point mutations and deletions into conserved residues of RBP1b TS, and evaluated their effect in the relative mitochondria/chloroplast targeting, using a novel GFP quantitative approach supported by statistical analyses. Mutations and deletions of serine residues along the TS had no effect on the dual targeting of RBP1b, although chloroplast-targeting sequences are normally rich in serine residues. However, mutations of arginine and lysine at the N-terminal region reduced targeting to mitochondria, pointing to the involvement of positive residues in the protein targeting to this organelle. Deletion of the first part of the TS (amino acids 2 to 17) abolished RBP1b targeting to mitochondria, and the protein was localized to the chloroplasts and cytosol. When the second part of the TS (amino acids 18-30) was deleted, RBP1b was detected, but with lower intensity, in chloroplasts, mitochondria and cytosol. Therefore, the signal for RBP1b targeting to chloroplasts is located along the TS, and targeting to mitochondria depends on the first part of the TS. While the first part of RBP1b TS has the information to promote the protein dual targeting, the second part appears to be involved with the efficiency of the process.

Financial Support: CNPq and the Centre Nacional de La Recherche Scientifique (CNRS)- France



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