Rapidly evolving lamins in a chordate, Oikopleura dioica, with unusual nuclear architecture.

Metazoan lamins are implicated in the organization of numerous critical nuclear processes. Among chordates, the appendicularian, Oikopleura dioica, has an unusually short life cycle involving rapid growth through extensive recourse to endoreduplication, a characteristic more associated with some invertebrates. In some tissues, this is accompanied by the formation of elaborate, bilaterally symmetric nuclear morphologies associated with specific gene expression patterns. Lamin composition can mediate nuclear shape in spermiogenesis as well as during pathological and normal aging and we have analyzed the O. dioica lamin and intermediate filament (IF) complement, comparing it to that present in other deuterostomes. O. dioica has one lamin gene coding two splice variants. Both variants share with the sister class ascidians a highly reduced C-terminal tail region lacking the immunoglobulin fold, indicating this derivation occurred at the base of the urochordate lineage. The OdLamin2 variant has a unique insertion of 63 amino acids in the normally short N-terminal region and has a developmental expression profile corresponding to the occurrence of endocycling. O. dioica has 4 cytoplasmic IF proteins, IF-A, C, Dalpha, and Dbeta. No homologues to the ascidian IF-B or F proteins were identified, reinforcing the suggestion that these proteins are unique to ascidians. The degree of sequence evolution in the rod domains of O. dioica cytoplasmic IF proteins and their closest ascidian and vertebrate homologues was similar. In contrast, whereas the rate of lamin B rod domain sequence evolution has also been similar in vertebrates, cephalochordates and the sea urchin, faster rates have occurred among the urochordates, with the O. dioica lamin displaying a far greater rate than any other lamin.