| Structural highlights
Function
[NHP6A_YEAST] DNA-binding protein that induces severe bending of DNA. Required for DNA-binding by the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. Also augments the fidelity of transcription by RNA polymerase III independently of any role in the FACT complex. Required for transcriptional initiation fidelity of some but not all tRNA genes. Seems to be functionally redundant with NHP6B.[1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [11]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
NHP6A is a chromatin-associated protein from Saccharomyces cerevisiae belonging to the HMG1/2 family of non-specific DNA binding proteins. NHP6A has only one HMG DNA binding domain and forms relatively stable complexes with DNA. We have determined the solution structure of NHP6A and constructed an NMR-based model structure of the DNA complex. The free NHP6A folds into an L-shaped three alpha-helix structure, and contains an unstructured 17 amino acid basic tail N-terminal to the HMG box. Intermolecular NOEs assigned between NHP6A and a 15 bp 13C,15N-labeled DNA duplex containing the SRY recognition sequence have positioned the NHP6A HMG domain onto the minor groove of the DNA at a site that is shifted by 1 bp and in reverse orientation from that found in the SRY-DNA complex. In the model structure of the NHP6A-DNA complex, the N-terminal basic tail is wrapped around the major groove in a manner mimicking the C-terminal tail of LEF1. The DNA in the complex is severely distorted and contains two adjacent kinks where side chains of methionine and phenylalanine that are important for bending are inserted. The NHP6A-DNA model structure provides insight into how this class of architectural DNA binding proteins may select preferential binding sites.
Solution structure of the HMG protein NHP6A and its interaction with DNA reveals the structural determinants for non-sequence-specific binding.,Allain FH, Yen YM, Masse JE, Schultze P, Dieckmann T, Johnson RC, Feigon J EMBO J. 1999 May 4;18(9):2563-79. PMID:10228169[12]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Paull TT, Johnson RC. DNA looping by Saccharomyces cerevisiae high mobility group proteins NHP6A/B. Consequences for nucleoprotein complex assembly and chromatin condensation. J Biol Chem. 1995 Apr 14;270(15):8744-54. PMID:7721780
- ↑ Paull TT, Carey M, Johnson RC. Yeast HMG proteins NHP6A/B potentiate promoter-specific transcriptional activation in vivo and assembly of preinitiation complexes in vitro. Genes Dev. 1996 Nov 1;10(21):2769-81. PMID:8946917
- ↑ Moreira JM, Holmberg S. Chromatin-mediated transcriptional regulation by the yeast architectural factors NHP6A and NHP6B. EMBO J. 2000 Dec 15;19(24):6804-13. PMID:11118215 doi:http://dx.doi.org/10.1093/emboj/19.24.6804
- ↑ Formosa T, Eriksson P, Wittmeyer J, Ginn J, Yu Y, Stillman DJ. Spt16-Pob3 and the HMG protein Nhp6 combine to form the nucleosome-binding factor SPN. EMBO J. 2001 Jul 2;20(13):3506-17. PMID:11432837 doi:http://dx.doi.org/10.1093/emboj/20.13.3506
- ↑ Kruppa M, Moir RD, Kolodrubetz D, Willis IM. Nhp6, an HMG1 protein, functions in SNR6 transcription by RNA polymerase III in S. cerevisiae. Mol Cell. 2001 Feb;7(2):309-18. PMID:11239460
- ↑ Lopez S, Livingstone-Zatchej M, Jourdain S, Thoma F, Sentenac A, Marsolier MC. High-mobility-group proteins NHP6A and NHP6B participate in activation of the RNA polymerase III SNR6 gene. Mol Cell Biol. 2001 May;21(9):3096-104. PMID:11287614 doi:http://dx.doi.org/10.1128/MCB.21.9.3096-3104.2001
- ↑ Ruone S, Rhoades AR, Formosa T. Multiple Nhp6 molecules are required to recruit Spt16-Pob3 to form yFACT complexes and to reorganize nucleosomes. J Biol Chem. 2003 Nov 14;278(46):45288-95. Epub 2003 Sep 1. PMID:12952948 doi:http://dx.doi.org/10.1074/jbc.M307291200
- ↑ Mason PB, Struhl K. The FACT complex travels with elongating RNA polymerase II and is important for the fidelity of transcriptional initiation in vivo. Mol Cell Biol. 2003 Nov;23(22):8323-33. PMID:14585989
- ↑ Rhoades AR, Ruone S, Formosa T. Structural features of nucleosomes reorganized by yeast FACT and its HMG box component, Nhp6. Mol Cell Biol. 2004 May;24(9):3907-17. PMID:15082784
- ↑ Biswas D, Yu Y, Prall M, Formosa T, Stillman DJ. The yeast FACT complex has a role in transcriptional initiation. Mol Cell Biol. 2005 Jul;25(14):5812-22. PMID:15987999 doi:http://dx.doi.org/25/14/5812
- ↑ Kassavetis GA, Steiner DF. Nhp6 is a transcriptional initiation fidelity factor for RNA polymerase III transcription in vitro and in vivo. J Biol Chem. 2006 Mar 17;281(11):7445-51. Epub 2006 Jan 11. PMID:16407207 doi:http://dx.doi.org/10.1074/jbc.M512810200
- ↑ Allain FH, Yen YM, Masse JE, Schultze P, Dieckmann T, Johnson RC, Feigon J. Solution structure of the HMG protein NHP6A and its interaction with DNA reveals the structural determinants for non-sequence-specific binding. EMBO J. 1999 May 4;18(9):2563-79. PMID:10228169 doi:10.1093/emboj/18.9.2563
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