The antiproliferative activity of the murine interferon-inducible Ifi 200 proteins depends on the presence of two 200 amino acid domains.
Interferon-inducible proteins, p200, have a modular organization consisting of one (p203) or two (p202 and p204) 200 amino acid motifs, designated as type a or b domains. The relationship between this domain organization and the antiproliferative activity was investigated by generating a hybrid protein with the 204 a domain upstream from the 203 b domain. This 204a/203b protein inhibits the proliferation of transfected cells, delays G0/G1 progression into S phase following serum restimulation, and inhibits the E2F-mediated transcriptional activity. These results demonstrate for the first time that both a and b domains are needed for inhibition of proliferation by the Ifi 200 proteins.
Gribaudo
G
G
Department of Public Health and Microbiology, University of Turin, Italy.
Riera
L
L
De Andrea
M
M
Landolfo
S
S
D016475:3T3 Cells / Q000187:drug effects; D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D002455:Cell Division / Q000235:genetics*; D017124:Conserved Sequence; D005347:Fibroblasts / Q000187:drug effects; D016898:Interferon-alpha / Q000494:pharmacology; D051379:Mice; D008810:Mice, Inbred C57BL; D009687:Nuclear Proteins / Q000235:genetics* / Q000276:immunology / Q000378:metabolism*; D010750:Phosphoproteins / Q000235:genetics / Q000276:immunology / Q000378:metabolism; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D014162:Transfection
C489664:Ifi16 protein, mouse; C109045:Ifi203 protein, mouse; D016898:Interferon-alpha; D009687:Nuclear Proteins; D010750:Phosphoproteins; D011994:Recombinant Proteins