A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores

Article Abstract:

Analysis of the yeast nuclear pore protein, Nup84p, revealed five proteins forming a complex. Four of the five proteins were identified: Nup120p, Nup85p, Sec13p, and a homolog of the Sec13p (designated Sec13p-ProtA). Biochemical analysis and null disruption studies of the four proteins indicated the importance of the presence of the Sec13p and Sec13p-ProtA proteins within the Nup84p complex in nuclear membrane and nuclear pore formation.

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Combinatorial marking of cells and organelles with reconstituted fluorescent proteins

Article Abstract:

The reconstitution of green fluorescent protein (GFP), yellow fluorescent protein (YFP) and CFP previously split into two polypeptides yields fluorescent products when coexpressed in C. elegans. It can confirm cellular coexpression and identify cells expressing a previously uncharacterized promoter as the reconstitution involves two components.

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Bone formation: The nuclear matrix reloade

Article Abstract:

The nuclear matrix protein Satb2 is reported to repress Hoxa2 expression and acts with other regulatory proteins to promote osteoblast differentiation. A molecular mechanism is suggested that enables the integration of patterning and differentiation during bone formation.

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