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The anabaena sp. PCC 7120 exoproteome: Taking a peek outside the box

Title
The anabaena sp. PCC 7120 exoproteome: Taking a peek outside the box
Type
Article in International Scientific Journal
Year
2015
Authors
Oliveira, P
(Author)
Other
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Martins, NM
(Author)
Other
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Santos, M
(Author)
Other
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Couto, NAS
(Author)
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Wright, PC
(Author)
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Journal
Title: LifeImported from Authenticus Search for Journal Publications
Vol. 5
Pages: 130-163
ISSN: 0024-3019
Publisher: MDPI
Indexing
Publicação em ISI Web of Knowledge ISI Web of Knowledge
Pubmed / Medline
Scientific classification
CORDIS: Natural sciences > Biological sciences > Biology > Microbiology
Other information
Authenticus ID: P-00A-8EQ
Abstract (EN): The interest in examining the subset of proteins present in the extracellular milieu, the exoproteome, has been growing due to novel insights highlighting their role on extracellular matrix organization and biofilm formation, but also on homeostasis and development. The cyanobacterial exoproteome is poorly studied, and the role of cyanobacterial exoproteins on cell wall biogenesis, morphology and even physiology is largely unknown. Here, we present a comprehensive examination of the Anabaena sp. PCC 7120 exoproteome under various growth conditions. Altogether, 139 proteins belonging to 16 different functional categories have been identified. A large fraction (48%) of the identified proteins is classified as ¿hypothetical¿, falls into the ¿other categories¿ set or presents no similarity to other proteins. The evidence presented here shows that Anabaena sp. PCC 7120 is capable of outer membrane vesicle formation and that these vesicles are likely to contribute to the exoproteome profile. Furthermore, the activity of selected exoproteins associated with oxidative stress has been assessed, suggesting their involvement in redox homeostasis mechanisms in the extracellular space. Finally, we discuss our results in light of other cyanobacterial exoproteome studies and focus on the potential of exploring cyanobacteria as cell factories to produce and secrete selected proteins. © 2015 by the authors; licensee MDPI, Basel, Switzerland.
Language: English
Type (Professor's evaluation): Scientific
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