Many of the proteins that mediate transport into and out of the nucleus hav
e been structurally and functionally conserved throughout evolution. Here w
e describe the sequence and characterization of the human MOG1 gene. The MO
G1 gene was originally identified in Saccharomyces cerevisiae as a multi-co
py suppressor of conditional alleles of the yeast nuclear transport factor,
GSP1 (scRan) (Oki and Nishimoto (1998) Proc. Natl. Acad. Sci. USA 95, 1538
8-15393). A search of the expressed sequence tag database identified a puta
tive human protein that is 2.9% identical and 47% similar to the yeast prot
ein. Our experiments demonstrate that the human MOG1 message is expressed i
n a variety of tissue samples. Several experiments indicate that the human
MOG1 protein binds to both yeast and human Ran suggesting functional conser
vation between the yeast and human MOG1 proteins. Furthermore, hMOG1a, like
scMOG1, is localized throughout the cell but is concentrated within the nu
cleus. Consistent with these findings, hMOG1a can partially complement the
growth defect present in yeast MOG1 deletion cells. Taken together, our fin
dings suggest that MOG1 is an evolutionarily conserved Ran binding protein
that could play a role in regulating nuclear protein trafficking. (C) 2001
Elsevier Science B.V. All rights reserved.