The highly conserved orthopoxvirus 68k ankyrin-like protein is part of a cellular SCF ubiquitin ligase complex.
The 68k ankyrin-like protein (68k-ank) of unknown function is highly conserved among orthopoxviruses and contains ankyrin repeats and an F-box-like domain. We performed a yeast-two-hybrid screen with 68k-ank to find interacting proteins. From a human and a murine cDNA library, 99% of the interaction partners were S-phase kinase-associated protein 1a (Skp1a), a part of the SCF ubiquitin ligase complex. 68k-ank co-immunoprecipitated with components of the endogenous, mammalian SCF ubiquitin ligase. This interaction was F-box domain dependent and could also be observed in infected cells, indicating that SCF complex formation might be important for the viral life cycle.
Sperling
Karin M
KM
Paul-Ehrlich-Institut, Department of Virology, Paul-Ehrlich-Strasse 51-59, 63225 Langen, Germany. speka@pei.de
Schwantes
Astrid
A
Schnierle
Barbara S
BS
Sutter
Gerd
G
D000595:Amino Acid Sequence; D000818:Animals; D017487:Ankyrins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017124:Conserved Sequence; D044782:F-Box Motifs / Q000235:genetics; D015723:Gene Library; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D018155:Orthopoxvirus / Q000235:genetics / Q000378:metabolism*; D044843:SKP Cullin F-Box Protein Ligases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D020798:Two-Hybrid System Techniques; D014616:Vaccinia virus / Q000235:genetics / Q000378:metabolism
D017487:Ankyrins; D044843:SKP Cullin F-Box Protein Ligases