Nuclear factor Y gene transcriptions

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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. 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.
  2. "Entrez Gene: NFYA nuclear transcription factor Y, alpha".
  3. 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.
  4. 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.
  5. 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.
  6. 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. 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.
  8. 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.
  9. 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.

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