The TrpA protein of Trichodesmium erythraeum IMS101 is a non-fibril-forming collagen and a component of the outer sheath

Abstract

Collagen molecules are structural in nature and primarily found in eukaryotic, multicellular organisms. Recently, a collagen-like protein, TrpA, was identified and characterized in the marine cyanobacterium Trichodesmium erythraeum IMS 101, and it was shown to be involved in maintaining the structural integrity of the trichomes. The TrpA protein contains one glycine interruption in the otherwise perfectly uninterrupted collagenous domain. In this study, we used phylogenetic analysis to determine that the TrpA protein sequence is most closely associated with non-fibril-forming collagen proteins. Structural modelling and circular dichroism data suggest that the glycine insertion decreases the stability of TrpA compared to uninterrupted collagen sequences. Additionally, scanning electron microscopy revealed that TrpA is expressed entirely on the surface of the trichomes, with no specific pattern of localization. These data indicate that the TrpA protein is part of the outer sheath of this organism. As such, this protein may function to promote adhesion between individual T. erythraeum trichomes, and between this organism and heterotrophic bacteria found in the same environment.

Soil organic matter and the extracellular microbial matrix show contrasting responses to C and N availability

“… Friedel and Scheller (2002) attributed high Asx and Ser to contributions from fungal cell walls ( Wagner and Mutatkar, 1968 ). The large increases in relative abundances of Pro and Gly in EPS suggest structural importance, both fulfilling formative roles in collagen and implicated in the adhesion between Trichodesmium erythraeum and heterotrophic bacteria in the marine environment ( Price et al., 2014 ). Proline and glycine rich domains also impart elasticity to elastin ( Le et al., 2013 ) and the glycoprotein fibrillin ( Mariko et al., 2010 ).…”

Curing Functions and Medical Applications of Microalgae

“…The phylogenetic evaluation confirmed that the protein collection of TrpA confirmed a excessive courting with collagen proteins, now no longer forming fibril. Scanning electron microscopy (SEM) outcomes confirmed the expression of TrpA on trichome surface, without a regular localization pattern (Price et al, 2014).…”

Bioactive substances and potentiality of marine microalgae

“…showed the expression of TrpA on trichome surface, with no typical localization pattern (Price et al, 2014). It has been reported that the TrpA gene showed expression at various growth stages, indicating its necessity for T. erythraeum growth.…”

“…The phylogenetic analysis showed that the protein sequence of TrpA showed a high relationship with collagen proteins, not forming fibril. Scanning electron microscopy (SEM) results showed the expression of TrpA on trichome surface, with no typical localization pattern (Price et al., 2014 ). It has been reported that the TrpA gene showed expression at various growth stages, indicating its necessity for T. erythraeum growth.…”