| Full text | |
| Author(s): |
Dias, Renata O.
[1]
;
Via, Allegra
[2, 3]
;
Brandao, Marcelo M.
[4]
;
Tramontano, Anna
[2, 3]
;
Silva-Filho, Marcio C.
[1]
Total Authors: 5
|
| Affiliation: | [1] Univ Sao Paulo, Escola Super Agr Luiz de Queiroz, Dept Genet, BR-13418900 Piracicaba, SP - Brazil
[2] Univ Roma La Sapienza, Fdn Cenci Bolognetti, Dept Phys, I-00185 Rome - Italy
[3] Univ Roma La Sapienza, Fdn Cenci Bolognetti, Ist Pasteur, I-00185 Rome - Italy
[4] Univ Estadual Campinas, Ctr Biol Mol & Engn Genet, BR-13083875 Campinas, SP - Brazil
Total Affiliations: 4
|
| Document type: | Journal article |
| Source: | Insect Biochemistry and Molecular Biology; v. 58, p. 1-11, MAR 2015. |
| Web of Science Citations: | 5 |
| Abstract | |
Trypsins and chymotrypsins are well-studied serine peptidases that cleave peptide bonds at the carboxyl side of basic and hydrophobic L-amino acids, respectively. These enzymes are largely responsible for the digestion of proteins. Three primary processes regulate the activity of these peptidases: secretion, precursor (zymogen) activation and substrate-binding site recognition. Here, we present a detailed phylogenetic analysis of trypsins and chymotrypsins in three orders of holometabolous insects and reveal divergent characteristics of Lepidoptera enzymes in comparison with those of Coleoptera and Diptera. In particular, trypsin subsite S1 was more hydrophilic in Lepidoptera than in Coleoptera and Diptera, whereas subsites S2-S4 were more hydrophobic, suggesting different substrate preferences. Furthermore, Lepidoptera displayed a lineage-specific trypsin group belonging only to the Noctuidae family. Evidence for facilitated trypsin auto-activation events were also observed in all the insect orders studied, with the characteristic zymogen activation motif complementary to the trypsin active site. In contrast, insect chymotrypsins did not seem to have a peculiar evolutionary history with respect to their mammal counterparts. Overall, our findings suggest that the need for fast digestion allowed holometabolous insects to evolve divergent groups of peptidases with high auto-activation rates, and highlight that the evolution of trypsins led to a most diverse group of enzymes in Lepidoptera. (C) 2015 Elsevier Ltd. All rights reserved. (AU) | |
| FAPESP's process: | 12/03040-0 - Evolution and characterization of serine protease gene family and its association with the feeding behavior in Noctuidae moths |
| Grantee: | Renata de Oliveira Dias |
| Support Opportunities: | Scholarships abroad - Research Internship - Doctorate |
| FAPESP's process: | 11/00417-3 - System biology techniques applied to the agriculture: transcriptomes and interactomes analyses |
| Grantee: | Marcelo Mendes Brandao |
| Support Opportunities: | Research Grants - Young Investigators Grants |
| FAPESP's process: | 10/17110-5 - Characterization of molecular bases involved in the polifagism of herbivore insect |
| Grantee: | Renata de Oliveira Dias |
| Support Opportunities: | Scholarships in Brazil - Doctorate |
| FAPESP's process: | 08/52067-3 - Herbivory and intracellular transport of proteins |
| Grantee: | Márcio de Castro Silva Filho |
| Support Opportunities: | Program for Research on Bioenergy (BIOEN) - Thematic Grants |