caa a22 4500 46318646X CHVBK 20180406164854.0 cr unu---uuuuu 170326e20071101xx s 000 0 eng 10.1007/s00726-006-0482-z doi (NATIONALLICENCE)springer-10.1007/s00726-006-0482-z Molecular cloning of a structural homolog of YY1AP, a coactivator of the multifunctional transcription factor YY1 [Elektronische Daten] [T. Ohtomo, T. Horii, M. Nomizu, T. Suga, J. Yamada] Summary.: YY1 is a multifunctional transcription factor that activates or represses gene transcription depending on interactions with other regulatory proteins that include coactivator YY1AP. Here, we describe the cloning of a novel homolog of YY1AP, referred to as YARP, from the human neuroblastoma cell line SK-N-SH. The cloned cDNA encoded a 2240 amino acid protein that contained a domain which was 97% homologous to an entire YY1AP sequence of 739 amino acids. Two splice variants, YARP2 and YARP3, were also cloned. Northern blotting demonstrated the YARP mRNA (∼10 kb), which was increased 1.7-fold after dibutyryl cAMP-induced neural differentiation of the cells. Presence of YARP mRNA was also confirmed in human tissues such as the heart, brain and placenta. Bioinformatic analysis predicted various functional motifs in the YARP structure, including nuclear localization signals and domains associated with protein-protein interactions (PAH2), DNA-binding (SANT), and chromatin assembly (nucleoplasmin-like), outside the YY1AP-homology domain. Thus, we propose that YARP is multifunctional and plays not only a role analogous to YY1AP, but also its own specific roles in DNA-utilizing processes such as transcription. Springer-Verlag, 2007 Keywords: YY1-associated protein - YARP - Dingo - GON4L - Gene expression - Human nationallicence dbcAMP : dibutyryl cyclic AMP nationallicence GAPDH : glyceraldehyde-3-phosphate dehydrogenase nationallicence RT : reverse transcription nationallicence YY1AP : YY1-associated protein nationallicence YARP : YY1AP-related protein (alias Dingo or GON4L) nationallicence Ohtomo T. Department of Clinical Biochemistry, Tokyo University of Pharmacy and Life Sciences, Tokyo, Japan aut Horii T. Department of Clinical Biochemistry, Tokyo University of Pharmacy and Life Sciences, Tokyo, Japan aut Nomizu M. Department of Clinical Biochemistry, Tokyo University of Pharmacy and Life Sciences, Tokyo, Japan aut Suga T. Department of Clinical Biochemistry, Tokyo University of Pharmacy and Life Sciences, Tokyo, Japan aut Yamada J. Department of Clinical Biochemistry, Tokyo University of Pharmacy and Life Sciences, Tokyo, Japan aut Amino Acids Springer-Verlag 33/4(2007-11-01), 645-652 0939-4451 33:4<645 2007 33 726 https://doi.org/10.1007/s00726-006-0482-z text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s00726-006-0482-z text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Ohtomo T. Department of Clinical Biochemistry, Tokyo University of Pharmacy and Life Sciences, Tokyo, Japan aut NATIONALLICENCE 700 1- Horii T. Department of Clinical Biochemistry, Tokyo University of Pharmacy and Life Sciences, Tokyo, Japan aut NATIONALLICENCE 700 1- Nomizu M. Department of Clinical Biochemistry, Tokyo University of Pharmacy and Life Sciences, Tokyo, Japan aut NATIONALLICENCE 700 1- Suga T. Department of Clinical Biochemistry, Tokyo University of Pharmacy and Life Sciences, Tokyo, Japan aut NATIONALLICENCE 700 1- Yamada J. Department of Clinical Biochemistry, Tokyo University of Pharmacy and Life Sciences, Tokyo, Japan aut NATIONALLICENCE 773 0- Amino Acids Springer-Verlag 33/4(2007-11-01), 645-652 0939-4451 33:4<645 2007 33 726 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer