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Alpha-actinin of the chlorarchiniophyte Bigelowiella natans.


ABSTRACT: The genome of the chlorarchiniophyte Bigelowiella natans codes for a protein annotated as an ?-actinin-like protein. Analysis of the primary sequence indicate that this protein has the same domain structure as other ?-actinins, a N-terminal actin-binding domain and a C-terminal calmodulin-like domain. These two domains are connected by a short rod domain, albeit long enough to form a single spectrin repeat. To analyse the functional properties of this protein, the full-length protein as well as the separate domains were cloned and isolated. Characerisation showed that the protein is capable of cross-linking actin filaments into dense bundles, probably due to dimer formation. Similar to human ?-actinin, calcium-binding occurs to the most N-terminal EF-hand motif in the calmodulin-like C-terminal domain. The results indicate that this Bigelowiella protein is a proper ?-actinin, with all common characteristics of a typical ?-actinin.

SUBMITTER: Backman L 

PROVIDER: S-EPMC5775757 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature

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Alpha-actinin of the chlorarchiniophyte <i>Bigelowiella natans</i>.

Backman Lars L  

PeerJ 20180117


The genome of the chlorarchiniophyte <i>Bigelowiella natans</i> codes for a protein annotated as an α-actinin-like protein. Analysis of the primary sequence indicate that this protein has the same domain structure as other α-actinins, a N-terminal actin-binding domain and a C-terminal calmodulin-like domain. These two domains are connected by a short rod domain, albeit long enough to form a single spectrin repeat. To analyse the functional properties of this protein, the full-length protein as w  ...[more]

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