Abstract:
:The protein kinase CK2 holoenzyme is composed of two regulatory beta- and two catalytic alpha- or alpha(')-subunits. There is ample evidence for the binding of individual subunits of CK2 to various cellular proteins and, moreover, for functions of the individual subunits, which are different from their roles in the holoenzyme. Here, we report that the regulatory cyclin H subunit of the cyclin H/cdk7/Mat1 complex was associated with a protein kinase activity, which shows some similarity with protein kinase CK2. Coimmunoprecipitation experiments supported the existence of complexes of cyclin H and CK2 in mammalian cells. Far Western blot experiments revealed that cyclin H bound to the alpha-subunit but not the alpha(')- and beta-subunits of CK2. Immunofluorescence analysis showed that cyclin H and CK2alpha were colocated in the nucleus. Although cyclin H functions as the regulatory subunit for the cyclin H/cdk7/Mat1 complex, it could not substitute the regulatory beta-subunit of CK2 in its regulatory function of the CK2 activity.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Faust M,Kartarius S,Schwindling SL,Montenarh Mdoi
10.1016/s0006-291x(02)00825-2subject
Has Abstractpub_date
2002-08-09 00:00:00pages
13-9issue
1eissn
0006-291Xissn
1090-2104pii
S0006291X02008252journal_volume
296pub_type
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