Nuclear factor Y gene transcriptions
Associate Editor(s)-in-Chief: Henry A. Hoff
The protein encoded by this gene is one subunit of a trimeric complex NF-Y, forming a highly conserved transcription factor that binds to CCAAT motifs in the promoter regions in a variety of genes.[1] Subunit NFYA associates with a tight dimer composed of the NFYB and NFYC subunits, resulting in a trimer that binds to DNA with high specificity and affinity. The sequence specific interactions of the complex are made by the NFYA subunit, suggesting a role as the regulatory subunit. In addition, there is evidence of post-transcriptional regulation in this gene product, either by protein degradation or control of translation. Further regulation is represented by alternative splicing in the glutamine-rich activation domain, with clear tissue-specific preferences for the two isoforms.[2]
NF-Y complex serves as a pioneer factor by promoting chromatin accessibility to facilitate other co-localizing cell type-specific transcription factors.[3]
NF-Y has also been implicated as a central player in transcription start site (TSS) selection in animals.[4] It safeguards the integrity of the nucleosome-depleted region and PIC localization at protein-coding gene promoters.
Human genes
Nuclear transcription factor Y subunit alpha is a protein that in humans is encoded by the NFYA gene.[5][6]
Interactions
NFYA has been shown to interact with Serum response factor[7] and ZHX1.[7][8] NFYA, NFYB and NFYC form the NFY complex and it has been shown that the NFY complex serves as a pioneer factor by promoting chromatin accessibility to facilitate other co-localizing cell type-specific transcription factors.[1]
Consensus sequences
Consensus sequences for the nuclear factor Y are CAATGGCG, CCAATGGAA and CCAATGGCA.[9]
Samplings
Copying an apparent consensus sequence for the NFY CCAATGG(A/C)(A/G) and putting it in "⌘F" finds none located between ZSCAN22 and none between ZNF497 and A1BG as can be found by the computer programs.
See also
References
- ↑ 1.0 1.1 Oldfield AJ, Yang P, Conway AE, Cinghu S, Freudenberg JM, Yellaboina S, Jothi R (September 2014). "Histone-fold domain protein NF-Y promotes chromatin accessibility for cell type-specific master transcription factors". Molecular Cell. 55 (5): 708–22. doi:10.1016/j.molcel.2014.07.005. PMC 4157648. PMID 25132174.
- ↑ "Entrez Gene: NFYA nuclear transcription factor Y, alpha".
- ↑ Oldfield AJ, Yang P, Conway AE, Cinghu S, Freudenberg JM, Yellaboina S, Jothi R (September 2014). "Histone-fold domain protein NF-Y promotes chromatin accessibility for cell type-specific master transcription factors". Molecular Cell. 55 (5): 708–22. doi:10.1016/j.molcel.2014.07.005. PMC 4157648. PMID 25132174.
- ↑ Oldfield AJ, Henriques T, Burkholder AB, Paulet D, Cinghu S, Yang P, Scruggs BS, Lavender CA, Kumar D, Bennett B, Rivals E (2019-07-11). "NF-Y controls fidelity of transcription initiation at gene promoters through maintenance of the nucleosome-depleted region". Nature Communications. 10 (1): 3072. doi:10.1038/s41467-019-10905-7. PMC 6624317 Check
|pmc=value (help). PMID 31296853. - ↑ Li XY, Mattei MG, Zaleska-Rutczynska Z, Hooft van Huijsduijnen R, Figueroa F, Nadeau J, Benoist C, Mathis D (November 1991). "One subunit of the transcription factor NF-Y maps close to the major histocompatibility complex in murine and human chromosomes". Genomics. 11 (3): 630–4. doi:10.1016/0888-7543(91)90070-U. PMID 1774067.
- ↑ Maity SN, de Crombrugghe B (May 1998). "Role of the CCAAT-binding protein CBF/NF-Y in transcription". Trends in Biochemical Sciences. 23 (5): 174–8. doi:10.1016/S0968-0004(98)01201-8. PMID 9612081.
- ↑ 7.0 7.1 Yamada K, Osawa H, Granner DK (October 1999). "Identification of proteins that interact with NF-YA". FEBS Letters. 460 (1): 41–5. doi:10.1016/S0014-5793(99)01311-3. PMID 10571058.
- ↑ Yamada K, Printz RL, Osawa H, Granner DK (August 1999). "Human ZHX1: cloning, chromosomal location, and interaction with transcription factor NF-Y". Biochemical and Biophysical Research Communications. 261 (3): 614–21. doi:10.1006/bbrc.1999.1087. PMID 10441475.
- ↑ D. W. Yao, J. Luo, Q. Y. He, J. Li, H. Wang, H. B. Shi, H. F. Xu, M. Wang and J. J. Loor (May 2016). "Characterization of the liver X receptor-dependent regulatory mechanism of goat stearoyl-coenzyme A desaturase 1 gene by linoleic acid". Journal of Dairy Science. 99 (5): 3945–3957. doi:10.3168/jds.2015-10601. PMID 26947306. Retrieved 5 September 2020.