Functional Analysis of CP2-Like Domain and SAM-Like Domain in TFCP2L1, Novel Pluripotency Factor of Embryonic Stem Cells
- Appl Biochem Biotechnol. 2016 Jun;179(4):650-8. doi: 10.1007/s12010-016-2021-z.
- 1. School of Chemistry and Biochemistry and Graduate School of Biochemistry, Yeungnam University, Gyeongsan, Republic of Korea.
- 2. School of Chemistry and Biochemistry and Graduate School of Biochemistry, Yeungnam University, Gyeongsan, Republic of Korea. [email protected].
TFCP2L1 is a transcription factor that facilitates establishment and maintenance of pluripotency in embryonic stem cells by forming a complex transcriptional network with other Transcription Factors (OCT4, SOX2, and NANOG). TFCP2L1 contains two distinct domains, the CP2-like domain at the N-terminus and the SAM-like domain at the C-terminus. In this study, we found that TFCP2L1 is hexamerized in solution via the C-terminal SAM-like domain. We also found that homo-oligomerization of SAM-like domain is dependent on the concentration of the proteins. Finally, we found that TFCP2L1 binds directly to DNA via the N-terminal CP2-like domain.