Open AccessSecretion of small proteins is species‐specific within Aspergillus sp
Author(s) -
Valette Nicolas,
BenoitGelber Isabelle,
Falco Marcos Di,
Wiebenga Ad,
Vries Ronald P.,
Gelhaye Eric,
MorelRouhier Mélanie
Publication year - 2017
Publication title -
microbial biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.287
H-Index - 74
ISSN - 1751-7915
DOI - 10.1111/1751-7915.12361
Subject(s) - context (archaeology) , biochemistry , secretion , enzyme , signal peptide , reactive oxygen species , amino acid , secretory protein , lytic cycle , chemistry , biology , peptide sequence , gene , genetics , paleontology , virus
Summary Small secreted proteins ( SSP ) have been defined as proteins containing a signal peptide and a sequence of less than 300 amino acids. In this analysis, we have compared the secretion pattern of SSP s among eight aspergilli species in the context of plant biomass degradation and have highlighted putative interesting candidates that could be involved in the degradative process or in the strategies developed by fungi to resist the associated stress that could be due to the toxicity of some aromatic compounds or reactive oxygen species released during degradation. Among these candidates, for example, some stress‐related superoxide dismutases or some hydrophobic surface binding proteins (HsbA) are specifically secreted according to the species . Since these latter proteins are able to recruit lytic enzymes to the surface of hydrophobic solid materials and promote their degradation, a synergistic action of HsbA with the degradative system may be considered and need further investigations. These SSP s could have great applications in biotechnology by optimizing the efficiency of the enzymatic systems for biomass degradation.