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Publication : Human and mouse MOK2 proteins are associated with nuclear ribonucleoprotein components and bind specifically to RNA and DNA through their zinc finger domains.

First Author  Arranz V Year  1997
Journal  Mol Cell Biol Volume  17
Issue  4 Pages  2116-26
PubMed ID  9121460 Mgi Jnum  J:39425
Mgi Id  MGI:86807 Doi  10.1128/mcb.17.4.2116
Citation  Arranz V, et al. (1997) Human and mouse MOK2 proteins are associated with nuclear ribonucleoprotein components and bind specifically to RNA and DNA through their zinc finger domains. Mol Cell Biol 17(4):2116-26
abstractText  The human and murine MOK2 ortholog genes that are preferentially expressed in brain and testis tissues encode two different Kruppel-like zinc finger proteins. In this paper, we show that the MOK2 proteins are mainly associated with nuclear ribonucleoprotein components, including the nucleoli and extranucleolar structures, and exhibit specific RNA homopolymer binding activities. Moreover, we have identified an identical 18-bp specific DNA binding sequence for both MOK2 proteins using a pool of random sequence oligonucleotides. The DNA binding domain is localized in the seven adjacent zinc finger motifs, which show 94% identity between human and murine proteins. Taken together, these results establish that the MOK2 proteins are able to recognize both DNA and RNA through their zinc fingers. This dual affinity and the subnuclear localization suggest that MOK2 may play roles in transcription, as well as in the posttranscriptional regulation processes of specific genes.
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