Enhancing QA systems with complex temporal question processing capabilities

This paper presents a multilayered architecture that enhances the capabilities of current QA systems and allows different types of complex questions or queries to be processed. The answers to these questions need to be gathered from factual information scattered throughout different documents. Specifically, we designed a specialized layer to process the different types of temporal questions. Complex temporal questions are first decomposed into simple questions, according to the temporal relations expressed in the original question. In the same way, the answers to the resulting simple questions are recomposed, fulfilling the temporal restrictions of the original complex question. A novel aspect of this approach resides in the decomposition which uses a minimal quantity of resources, with the final aim of obtaining a portable platform that is easily extensible to other languages. In this paper we also present a methodology for evaluation of the decomposition of the questions as well as the ability of the implemented temporal layer to perform at a multilingual level. The temporal layer was first performed for English, then evaluated and compared with: a) a general purpose QA system (F-measure 65.47% for QA plus English temporal layer vs. 38.01% for the general QA system), and b) a well-known QA system. Much better results were obtained for temporal questions with the multilayered system. This system was therefore extended to Spanish and very good results were again obtained in the evaluation (F-measure 40.36% for QA plus Spanish temporal layer vs. 22.94% for the general QA system).

Gene cloning, molecular modeling, and phylogenetics of serine protease P32 and serine carboxypeptidase SCP1 from nematophagous fungi Pochonia rubescens and Pochonia chlamydosporia

The fungi Pochonia chlamydosporia and Pochonia rubescens are parasites of nematode eggs and thus are biocontrol agents of nematodes. Proteolytic enzymes such as the S8 proteases VCP1 and P32, secreted during the pathogenesis of nematode eggs, are major virulence factors in these fungi. Recently, expression of these enzymes and of SCP1, a new putative S10 carboxypeptidase, was detected during endophytic colonization of barley roots by these fungi. In our study, we cloned the genomic and mRNA sequences encoding P32 from P. rubescens and SCP1 from P. chlamydosporia. P32 showed a high homology with the serine proteases Pr1A from the entomopathogenic fungus Metarhizium anisopliae and VCP1 from P. chlamydosporia (86% and 76% identity, respectively). However, the catalytic pocket of P32 showed differences in the amino acids of the substrate-recognition sites compared with the catalytic pockets of Pr1A and VCP1 proteases. Phylogenetic analysis of P32 suggests a common ancestor with protease Pr1A. SCP1 displays the characteristic features of a member of the S10 family of serine proteases. Phylogenetic comparisons show that SCP1 and other carboxypeptidases from filamentous fungi have an origin different from that of yeast vacuolar serine carboxypeptidases. Understanding protease genes from nematophagous fungi is crucial for enhancing the biocontrol potential of these organisms.