Novel interaction interfaces mediate the interaction between the NEIL1 DNA glycosylase and mitochondrial transcription factor A

Sharma, Nidhi; Thompson, Marlo K.; Arrington, Jennifer F.; Terry, Dava M.; Chakravarthy, Srinivas; Prevelige, Peter E.; Prakash, Aishwarya

doi:10.3389/fcell.2022.893806

Novel interaction interfaces mediate the interaction between the NEIL1 DNA glycosylase and mitochondrial transcription factor A

Journal Article · Fri Jul 22 00:00:00 EDT 2022 · Frontiers in Cell and Developmental Biology

DOI:https://doi.org/10.3389/fcell.2022.893806· OSTI ID:1983086

Sharma, Nidhi ^[1]; Thompson, Marlo K. ^[1]; Arrington, Jennifer F. ^[1]; Terry, Dava M. ^[1]; Chakravarthy, Srinivas ^[2]; Prevelige, Peter E. ^[3]; Prakash, Aishwarya ^[1]

Univ. of South Alabama, Mobile, AL (United States)
Illinois Institute of Technology, Chicago, IL (United States)
Univ. of Alabama, Birmingham, AL (United States)

The maintenance of human mitochondrial DNA (mtDNA) is critical for proper cellular function as damage to mtDNA, if left unrepaired, can lead to a diverse array of pathologies. Of the pathways identified to participate in DNA repair within the mitochondria, base excision repair (BER) is the most extensively studied. Protein-protein interactions drive the step-by-step coordination required for the successful completion of this pathway and are important for crosstalk with other mitochondrial factors involved in genome maintenance. Human NEIL1 is one of seven DNA glycosylases that initiates BER in both the nuclear and mitochondrial compartments. In the current work, we scrutinized the interaction between NEIL1 and mitochondrial transcription factor A (TFAM), a protein that is essential for various aspects of mtDNA metabolism. We note, for the first time, that both the N- and C- terminal domains of NEIL1 interact with TFAM revealing a unique NEIL1 protein-binding interface. The interaction between the two proteins, as observed biochemically, appears to be transient and is most apparent at concentrations of low salt. The presence of DNA (or RNA) also positively influences the interaction between the two proteins, and molar mass estimates indicate that duplex DNA is required for complex formation at higher salt concentrations. Hydrogen deuterium exchange mass spectrometry data reveal that both proteins exchange less deuterium upon DNA binding, indicative of an interaction, and the addition of NEIL1 to the TFAM-DNA complex alters the interaction landscape. The transcriptional activity of TFAM appears to be independent of NEIL1 expression under normal cellular conditions, however, in the presence of DNA damage, we observe a significant reduction in the mRNA expression of TFAM-transcribed mitochondrial genes in the absence of NEIL1. Overall, our data indicate that the interaction between NEIL1 and TFAM can be modulated by local environment such as salt concentrations, protein availability, the presence of nucleic acids, as well as the presence of DNA damage.

View Accepted Manuscript (DOE)

Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Organization:: USDOE Office of Science (SC); National Institutes of Environmental Health Sciences (NIEHS); National Institutes of Health (NIH)

Grant/Contract Number:: AC02-06CH11357

OSTI ID:: 1983086

Journal Information:: Frontiers in Cell and Developmental Biology, Journal Name: Frontiers in Cell and Developmental Biology Vol. 10; ISSN 2296-634X

Publisher:: Frontiers Media S.A.Copyright Statement

Country of Publication:: United States

Language:: English

References (89)

Base Excision Repair in the Mitochondria Prakash, Aishwarya; Doublié, Sylvie Journal of Cellular Biochemistry, Vol. 116, Issue 8 https://doi.org/10.1002/jcb.25103	journal	June 2015
Methods for the detection and analysis of protein–protein interactions Berggård, Tord; Linse, Sara; James, Peter PROTEOMICS, Vol. 7, Issue 16 https://doi.org/10.1002/pmic.200700131	journal	August 2007
SAXSMoW 2.0: Online calculator of the molecular weight of proteins in dilute solution from experimental SAXS data measured on a relative scale Piiadov, Vassili; Ares de Araújo, Evandro; Oliveira Neto, Mario Protein Science, Vol. 28, Issue 2 https://doi.org/10.1002/pro.3528	journal	December 2018
Functions of disordered regions in mammalian early base excision repair proteins Hegde, Muralidhar L.; Hazra, Tapas K.; Mitra, Sankar Cellular and Molecular Life Sciences, Vol. 67, Issue 21 https://doi.org/10.1007/s00018-010-0485-5	journal	August 2010
Distribution of methyl and ethyl adducts following alkylation with monofunctional alkylating agents Beranek, David T. Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis, Vol. 231, Issue 1 https://doi.org/10.1016/0027-5107(90)90173-2	journal	July 1990
Mitochondrial DNA: Radically free of free-radical driven mutations Kauppila, Johanna H. K.; Stewart, James B. Biochimica et Biophysica Acta (BBA) - Bioenergetics, Vol. 1847, Issue 11 https://doi.org/10.1016/j.bbabio.2015.06.001	journal	November 2015
Mitochondrial DNA nucleoid structure Bogenhagen, Daniel F. Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms, Vol. 1819, Issue 9-10 https://doi.org/10.1016/j.bbagrm.2011.11.005	journal	September 2012
Mitochondrial transcription factor A regulates mitochondrial transcription initiation, DNA packaging, and genome copy number Campbell, Christopher T.; Kolesar, Jill E.; Kaufman, Brett A. Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms, Vol. 1819, Issue 9-10 https://doi.org/10.1016/j.bbagrm.2012.03.002	journal	September 2012
Structural insight into the mitochondrial protein import system Endo, Toshiya; Yamano, Koji; Kawano, Shin Biochimica et Biophysica Acta (BBA) - Biomembranes, Vol. 1808, Issue 3 https://doi.org/10.1016/j.bbamem.2010.07.018	journal	March 2011
Protein Flexibility and Synergy of HMG Domains Underlie U-Turn Bending of DNA by TFAM in Solution Rubio-Cosials, Anna; Battistini, Federica; Gansen, Alexander Biophysical Journal, Vol. 114, Issue 10 https://doi.org/10.1016/j.bpj.2017.11.3743	journal	May 2018
Machine Learning Methods for X-Ray Scattering Data Analysis from Biomacromolecular Solutions Franke, Daniel; Jeffries, Cy M.; Svergun, Dmitri I. Biophysical Journal, Vol. 114, Issue 11 https://doi.org/10.1016/j.bpj.2018.04.018	journal	June 2018
Base excision repair and cancer Wallace, Susan S.; Murphy, Drew L.; Sweasy, Joann B. Cancer Letters, Vol. 327, Issue 1-2 https://doi.org/10.1016/j.canlet.2011.12.038	journal	December 2012
Recognition of the oxidized lesions spiroiminodihydantoin and guanidinohydantoin in DNA by the mammalian base excision repair glycosylases NEIL1 and NEIL2 Hailer, M. Katie; Slade, Peter G.; Martin, Brooke D. DNA Repair, Vol. 4, Issue 1 https://doi.org/10.1016/j.dnarep.2004.07.006	journal	January 2005
Non-specific DNA binding interferes with the efficient excision of oxidative lesions from chromatin by the human DNA glycosylase, NEIL1 Odell, Ian D.; Newick, Kheng; Heintz, Nicholas H. DNA Repair, Vol. 9, Issue 2 https://doi.org/10.1016/j.dnarep.2009.11.005	journal	February 2010
RPA physically interacts with the human DNA glycosylase NEIL1 to regulate excision of oxidative DNA base damage in primer-template structures Theriot, Corey A.; Hegde, Muralidhar L.; Hazra, Tapas K. DNA Repair, Vol. 9, Issue 6 https://doi.org/10.1016/j.dnarep.2010.02.014	journal	June 2010
The mitochondrial transcription factor A functions in mitochondrial base excision repair Canugovi, Chandrika; Maynard, Scott; Bayne, Anne-Cécile V. DNA Repair, Vol. 9, Issue 10 https://doi.org/10.1016/j.dnarep.2010.07.009	journal	October 2010
Biochemical mapping of human NEIL1 DNA glycosylase and AP lyase activities Vik, Erik Sebastian; Alseth, Ingrun; Forsbring, Monika DNA Repair, Vol. 11, Issue 9 https://doi.org/10.1016/j.dnarep.2012.07.002	journal	September 2012
Alkyladenine DNA glycosylase (AAG) localizes to mitochondria and interacts with mitochondrial single-stranded binding protein (mtSSB) van Loon, Barbara; Samson, Leona D. DNA Repair, Vol. 12, Issue 3 https://doi.org/10.1016/j.dnarep.2012.11.009	journal	March 2013
Genome and cancer single nucleotide polymorphisms of the human NEIL1 DNA glycosylase: Activity, structure, and the effect of editing Prakash, Aishwarya; Carroll, Brittany L.; Sweasy, Joann B. DNA Repair, Vol. 14 https://doi.org/10.1016/j.dnarep.2013.12.003	journal	February 2014
Mitochondrial genome maintenance in health and disease Copeland, William C.; Longley, Matthew J. DNA Repair, Vol. 19 https://doi.org/10.1016/j.dnarep.2014.03.010	journal	July 2014
The C-terminal tail of the NEIL1 DNA glycosylase interacts with the human mitochondrial single-stranded DNA binding protein Sharma, Nidhi; Chakravarthy, Srinivas; Longley, Matthew J. DNA Repair, Vol. 65 https://doi.org/10.1016/j.dnarep.2018.02.012	journal	May 2018
Acetylation of oxidized base repair-initiating NEIL1 DNA glycosylase required for chromatin-bound repair complex formation in the human genome increases cellular resistance to oxidative stress Sengupta, Shiladitya; Yang, Chunying; Hegde, Muralidhar L. DNA Repair, Vol. 66-67 https://doi.org/10.1016/j.dnarep.2018.04.001	journal	June 2018
Recognition of DNA adducts by edited and unedited forms of DNA glycosylase NEIL1 Minko, Irina G.; Vartanian, Vladimir L.; Tozaki, Naoto N. DNA Repair, Vol. 85 https://doi.org/10.1016/j.dnarep.2019.102741	journal	January 2020
DNA polymerase β outperforms DNA polymerase γ in key mitochondrial base excision repair activities Baptiste, Beverly A.; Baringer, Stephanie L.; Kulikowicz, Tomasz DNA Repair, Vol. 99 https://doi.org/10.1016/j.dnarep.2021.103050	journal	March 2021
DNA damage related crosstalk between the nucleus and mitochondria Saki, Mohammad; Prakash, Aishwarya Free Radical Biology and Medicine, Vol. 107 https://doi.org/10.1016/j.freeradbiomed.2016.11.050	journal	June 2017
Conformational Dynamics of Damage Processing by Human DNA Glycosylase NEIL1 Kladova, Olga A.; Grin, Inga R.; Fedorova, Olga S. Journal of Molecular Biology, Vol. 431, Issue 6 https://doi.org/10.1016/j.jmb.2019.01.030	journal	March 2019
RNA Editing of the Human DNA Glycosylase NEIL1 Alters Its Removal of 5-Hydroxyuracil Lesions in DNA Yeo, Jongchan; Lotsof, Elizabeth R.; Anderson-Steele, Brittany M. Biochemistry, Vol. 60, Issue 19 https://doi.org/10.1021/acs.biochem.1c00062	journal	April 2021
Superior Removal of Hydantoin Lesions Relative to Other Oxidized Bases by the Human DNA Glycosylase hNEIL1 Krishnamurthy, Nirmala; Zhao, Xiaobei; Burrows, Cynthia J. Biochemistry, Vol. 47, Issue 27 https://doi.org/10.1021/bi800160s	journal	June 2008
Mutation versus Repair: NEIL1 Removal of Hydantoin Lesions in Single-Stranded, Bulge, Bubble, and Duplex DNA Contexts Zhao, Xiaobei; Krishnamurthy, Nirmala; Burrows, Cynthia J. Biochemistry, Vol. 49, Issue 8 https://doi.org/10.1021/bi901852q	journal	March 2010
Domain Movements upon Activation of Phenylalanine Hydroxylase Characterized by Crystallography and Chromatography-Coupled Small-Angle X-ray Scattering Meisburger, Steve P.; Taylor, Alexander B.; Khan, Crystal A. Journal of the American Chemical Society, Vol. 138, Issue 20 https://doi.org/10.1021/jacs.6b01563	journal	May 2016
Biologically Relevant Chemical Reactions of N7-Alkylguanine Residues in DNA Gates, Kent S.; Nooner, Tony; Dutta, Sanjay Chemical Research in Toxicology, Vol. 17, Issue 7 https://doi.org/10.1021/tx049965c	journal	July 2004
Sequence and organization of the human mitochondrial genome Anderson, S.; Bankier, A. T.; Barrell, B. G. Nature, Vol. 290, Issue 5806 https://doi.org/10.1038/290457a0	journal	April 1981
Instability and decay of the primary structure of DNA Lindahl, Tomas Nature, Vol. 362, Issue 6422 https://doi.org/10.1038/362709a0	journal	April 1993
Accurate assessment of mass, models and resolution by small-angle scattering Rambo, Robert P.; Tainer, John A. Nature, Vol. 496, Issue 7446 https://doi.org/10.1038/nature12070	journal	April 2013
Distinct structural features of TFAM drive mitochondrial DNA packaging versus transcriptional activation Ngo, Huu B.; Lovely, Geoffrey A.; Phillips, Rob Nature Communications, Vol. 5, Issue 1 https://doi.org/10.1038/ncomms4077	journal	January 2014
The mitochondrial transcription and packaging factor Tfam imposes a U-turn on mitochondrial DNA Ngo, Huu B.; Kaiser, Jens T.; Chan, David C. Nature Structural & Molecular Biology, Vol. 18, Issue 11 https://doi.org/10.1038/nsmb.2159	journal	October 2011
Human mitochondrial transcription factor A induces a U-turn structure in the light strand promoter Rubio-Cosials, Anna; Sydow, Jasmin F.; Jiménez-Menéndez, Nereida Nature Structural & Molecular Biology, Vol. 18, Issue 11 https://doi.org/10.1038/nsmb.2160	journal	October 2011
Neil DNA glycosylases promote substrate turnover by Tdg during DNA demethylation Schomacher, Lars; Han, Dandan; Musheev, Michael U. Nature Structural & Molecular Biology, Vol. 23, Issue 2 https://doi.org/10.1038/nsmb.3151	journal	January 2016
Alkyladenine DNA glycosylase associates with transcription elongation to coordinate DNA repair with gene expression Montaldo, Nicola P.; Bordin, Diana L.; Brambilla, Alessandro Nature Communications, Vol. 10, Issue 1 https://doi.org/10.1038/s41467-019-13394-w	journal	November 2019
DNA repair glycosylase hNEIL1 triages damaged bases via competing interaction modes Liu, Menghao; Zhang, Jun; Zhu, Chenxu Nature Communications, Vol. 12, Issue 1 https://doi.org/10.1038/s41467-021-24431-y	journal	July 2021
POLG-related disorders and their neurological manifestations Rahman, Shamima; Copeland, William C. Nature Reviews Neurology, Vol. 15, Issue 1 https://doi.org/10.1038/s41582-018-0101-0	journal	November 2018
Consensus Bayesian assessment of protein molecular mass from solution X-ray scattering data Hajizadeh, Nelly R.; Franke, Daniel; Jeffries, Cy M. Scientific Reports, Vol. 8, Issue 1 https://doi.org/10.1038/s41598-018-25355-2	journal	May 2018
VolcaNoseR is a web app for creating, exploring, labeling and sharing volcano plots Goedhart, Joachim; Luijsterburg, Martijn S. Scientific Reports, Vol. 10, Issue 1 https://doi.org/10.1038/s41598-020-76603-3	journal	November 2020
The crystal structure of human endonuclease VIII-like 1 (NEIL1) reveals a zincless finger motif required for glycosylase activity Doublie, S.; Bandaru, V.; Bond, J. P. Proceedings of the National Academy of Sciences, Vol. 101, Issue 28 https://doi.org/10.1073/pnas.0402051101	journal	July 2004
The metabolic syndrome resulting from a knockout of the NEIL1 DNA glycosylase Vartanian, V.; Lowell, B.; Minko, I. G. Proceedings of the National Academy of Sciences, Vol. 103, Issue 6 https://doi.org/10.1073/pnas.0507444103	journal	January 2006
Super-resolution microscopy reveals that mammalian mitochondrial nucleoids have a uniform size and frequently contain a single copy of mtDNA Kukat, Christian; Wurm, Christian A.; Spåhr, Henrik Proceedings of the National Academy of Sciences, Vol. 108, Issue 33 https://doi.org/10.1073/pnas.1109263108	journal	August 2011
Cross-strand binding of TFAM to a single mtDNA molecule forms the mitochondrial nucleoid Kukat, Christian; Davies, Karen M.; Wurm, Christian A. Proceedings of the National Academy of Sciences, Vol. 112, Issue 36 https://doi.org/10.1073/pnas.1512131112	journal	August 2015
Tautomerization-dependent recognition and excision of oxidation damage in base-excision DNA repair Zhu, Chenxu; Lu, Lining; Zhang, Jun Proceedings of the National Academy of Sciences, Vol. 113, Issue 28 https://doi.org/10.1073/pnas.1604591113	journal	June 2016
Mitochondrial transcription factor A promotes DNA strand cleavage at abasic sites Xu, Wenyan; Boyd, Riley M.; Tree, Maya O. Proceedings of the National Academy of Sciences, Vol. 116, Issue 36 https://doi.org/10.1073/pnas.1911252116	journal	August 2019
Mitochondrial DNA damage is more extensive and persists longer than nuclear DNA damage in human cells following oxidative stress Yakes, F. M.; Van Houten, B. Proceedings of the National Academy of Sciences, Vol. 94, Issue 2 https://doi.org/10.1073/pnas.94.2.514	journal	January 1997
The C-terminal Domain (CTD) of Human DNA Glycosylase NEIL1 Is Required for Forming BERosome Repair Complex with DNA Replication Proteins at the Replicating Genome: DOMINANT NEGATIVE FUNCTION OF THE CTD Hegde, Pavana M.; Dutta, Arijit; Sengupta, Shiladitya Journal of Biological Chemistry, Vol. 290, Issue 34 https://doi.org/10.1074/jbc.M115.642918	journal	July 2015
Repair of Formamidopyrimidines in DNA Involves Different Glycosylases Hu, Jingping; de Souza-Pinto, Nadja C.; Haraguchi, Kazuhiro Journal of Biological Chemistry, Vol. 280, Issue 49 https://doi.org/10.1074/jbc.M508772200	journal	December 2005
The Human Werner Syndrome Protein Stimulates Repair of Oxidative DNA Base Damage by the DNA Glycosylase NEIL1 Das, Aditi; Boldogh, Istvan; Lee, Jae Wan Journal of Biological Chemistry, Vol. 282, Issue 36 https://doi.org/10.1074/jbc.M703343200	journal	September 2007
The Layered Structure of Human Mitochondrial DNA Nucleoids Bogenhagen, Daniel F.; Rousseau, Denis; Burke, Stephanie Journal of Biological Chemistry, Vol. 283, Issue 6 https://doi.org/10.1074/jbc.M708444200	journal	February 2008
Interaction of the Human DNA Glycosylase NEIL1 with Proliferating Cell Nuclear Antigen Dou, Hong; Theriot, Corey A.; Das, Aditi Journal of Biological Chemistry, Vol. 283, Issue 6 https://doi.org/10.1074/jbc.M709186200	journal	February 2008
Physical and Functional Interaction between Human Oxidized Base-specific DNA Glycosylase NEIL1 and Flap Endonuclease 1 Hegde, Muralidhar L.; Theriot, Corey A.; Das, Aditi Journal of Biological Chemistry, Vol. 283, Issue 40 https://doi.org/10.1074/jbc.M802712200	journal	July 2008
Long Patch Base Excision Repair in Mammalian Mitochondrial Genomes Szczesny, Bartosz; Tann, Anne W.; Longley, Matthew J. Journal of Biological Chemistry, Vol. 283, Issue 39 https://doi.org/10.1074/jbc.M803491200	journal	September 2008
The Mitochondrial Transcription Factor TFAM Coordinates the Assembly of Multiple DNA Molecules into Nucleoid-like Structures Kaufman, Brett A.; Durisic, Nela; Mativetsky, Jeffrey M. Molecular Biology of the Cell, Vol. 18, Issue 9 https://doi.org/10.1091/mbc.e07-05-0404	journal	September 2007
Human mitochondrial DNA is packaged with TFAM Alam, T. I. Nucleic Acids Research, Vol. 31, Issue 6 https://doi.org/10.1093/nar/gkg251	journal	March 2003
Structural analysis and DNA binding of the HMG domains of the human mitochondrial transcription factor A Gangelhoff, Todd A.; Mungalachetty, Purnima S.; Nix, Jay C. Nucleic Acids Research, Vol. 37, Issue 10 https://doi.org/10.1093/nar/gkp157	journal	March 2009
Transcriptional activation by mitochondrial transcription factor A involves preferential distortion of promoter DNA Malarkey, Christopher S.; Bestwick, Megan; Kuhlwilm, Jane E. Nucleic Acids Research, Vol. 40, Issue 2 https://doi.org/10.1093/nar/gkr787	journal	September 2011
Human mitochondrial transcription factors TFAM and TFB2M work synergistically in promoter melting during transcription initiation Ramachandran, Aparna; Basu, Urmimala; Sultana, Shemaila Nucleic Acids Research, Vol. 45, Issue 2 https://doi.org/10.1093/nar/gkw1157	journal	November 2016
Destabilization of the PCNA trimer mediated by its interaction with the NEIL1 DNA glycosylase Prakash, Aishwarya; Moharana, Kedar; Wallace, Susan S. Nucleic Acids Research https://doi.org/10.1093/nar/gkw1282	journal	December 2016
DNA specificities modulate the binding of human transcription factor A to mitochondrial DNA control region Cuppari, Anna; Fernández-Millán, Pablo; Battistini, Federica Nucleic Acids Research, Vol. 47, Issue 12 https://doi.org/10.1093/nar/gkz406	journal	May 2019
DNAproDB: an expanded database and web-based tool for structural analysis of DNA–protein complexes Sagendorf, Jared M.; Markarian, Nicholas; Berman, Helen M. Nucleic Acids Research https://doi.org/10.1093/nar/gkz889	journal	October 2019
Transient protein-protein interactions Acuner Ozbabacan, S. E.; Engin, H. B.; Gursoy, A. Protein Engineering Design and Selection, Vol. 24, Issue 9 https://doi.org/10.1093/protein/gzr025	journal	June 2011
Mitochondrial endogenous oxidative damage has been overestimated Michael Anson, R.; Hudson, Edgar; Bohr, Vilhelm A. The FASEB Journal, Vol. 14, Issue 2 https://doi.org/10.1096/fasebj.14.2.355	journal	February 2000
Base Excision Repair Krokan, H. E.; Bjoras, M. Cold Spring Harbor Perspectives in Biology, Vol. 5, Issue 4 https://doi.org/10.1101/cshperspect.a012583	journal	April 2013
BioXTAS RAW : improvements to a free open-source program for small-angle X-ray scattering data reduction and analysis Hopkins, Jesse Bennett; Gillilan, Richard E.; Skou, Soren Journal of Applied Crystallography, Vol. 50, Issue 5 https://doi.org/10.1107/S1600576717011438	journal	September 2017
PRIMUS: a Windows PC-based system for small-angle scattering data analysis Konarev, Petr V.; Volkov, Vladimir V.; Sokolova, Anna V. Journal of Applied Crystallography, Vol. 36, Issue 5, p. 1277-1282 https://doi.org/10.1107/s0021889803012779	journal	September 2003
Determination of the regularization parameter in indirect-transform methods using perceptual criteria Svergun, D. I. Journal of Applied Crystallography, Vol. 25, Issue 4, p. 495-503 https://doi.org/10.1107/s0021889892001663	journal	August 1992
Base Excision Repair, a Pathway Regulated by Posttranslational Modifications Carter, Rachel J.; Parsons, Jason L. Molecular and Cellular Biology, Vol. 36, Issue 10 https://doi.org/10.1128/MCB.00030-16	journal	May 2016
Protein–Protein Interactions in DNA Base Excision Repair Moor, N. A.; Lavrik, O. I. Biochemistry (Moscow), Vol. 83, Issue 4 https://doi.org/10.1134/S0006297918040120	journal	April 2018
Mitochondrial Machineries for Protein Import and Assembly Wiedemann, Nils; Pfanner, Nikolaus Annual Review of Biochemistry, Vol. 86, Issue 1 https://doi.org/10.1146/annurev-biochem-060815-014352	journal	June 2017
Mitochondria-Associated Proteostasis Ruan, Linhao; Wang, Yuhao; Zhang, Xi Annual Review of Biophysics, Vol. 49, Issue 1 https://doi.org/10.1146/annurev-biophys-121219-081604	journal	May 2020
Variable penetrance of metabolic phenotypes and development of high-fat diet-induced adiposity in NEIL1-deficient mice Sampath, Harini; Batra, Ayesha K.; Vartanian, Vladimir American Journal of Physiology-Endocrinology and Metabolism, Vol. 300, Issue 4 https://doi.org/10.1152/ajpendo.00387.2010	journal	April 2011
Protein-Protein Interaction Detection: Methods and Analysis Rao, V. Srinivasa; Srinivas, K.; Sujini, G. N. International Journal of Proteomics, Vol. 2014 https://doi.org/10.1155/2014/147648	journal	January 2014
The Antitumor Drug LB-100 Is a Catalytic Inhibitor of Protein Phosphatase 2A (PPP2CA) and 5 (PPP5C) Coordinating with the Active-Site Catalytic Metals in PPP5C D'Arcy, Brandon M.; Swingle, Mark R.; Papke, Cinta M. Molecular Cancer Therapeutics, Vol. 18, Issue 3 https://doi.org/10.1158/1535-7163.MCT-17-1143	journal	March 2019
Oxidative Damage in Mitochondrial DNA Is Not Extensive Lim, Kok Seong; Jeyaseelan, Kandiah; Whiteman, Matthew Annals of the New York Academy of Sciences, Vol. 1042, Issue 1 https://doi.org/10.1196/annals.1338.023	journal	May 2005
Mitochondrial Transcription Factor A (TFAM) Binds to RNA Containing 4-Way Junctions and Mitochondrial tRNA Brown, Timothy A.; Tkachuk, Ariana N.; Clayton, David A. PLOS ONE, Vol. 10, Issue 11 https://doi.org/10.1371/journal.pone.0142436	journal	November 2015
Phosphorylation Sites Identified in the NEIL1 DNA Glycosylase Are Potential Targets for the JNK1 Kinase Prakash, Aishwarya; Cao, Vy Bao; Doublié, Sylvie PLOS ONE, Vol. 11, Issue 8 https://doi.org/10.1371/journal.pone.0157860	journal	August 2016
High levels of TFAM repress mammalian mitochondrial DNA transcription in vivo Bonekamp, Nina A.; Jiang, Min; Motori, Elisa Life Science Alliance, Vol. 4, Issue 11 https://doi.org/10.26508/lsa.202101034	journal	August 2021
Mitochondrial DNA damage induced autophagy cell death and disease Houten, Bennett Van Frontiers in Bioscience, Vol. 21, Issue 1 https://doi.org/10.2741/4375	journal	January 2016
Higher Order Organization of the mtDNA: Beyond Mitochondrial Transcription Factor A Mishmar, Dan; Levin, Rotem; Naeem, Mansur M. Frontiers in Genetics, Vol. 10 https://doi.org/10.3389/fgene.2019.01285	journal	December 2019
Human DNA Glycosylase NEIL1’s Interactions with Downstream Repair Proteins Is Critical for Efficient Repair of Oxidized DNA Base Damage and Enhanced Cell Survival Hegde, Muralidhar; Hegde, Pavana; Arijit, Dutta Biomolecules, Vol. 2, Issue 4 https://doi.org/10.3390/biom2040564	journal	November 2012
HDX-MS: An Analytical Tool to Capture Protein Motion in Action Narang, Dominic; Lento, Cristina; J. Wilson, Derek Biomedicines, Vol. 8, Issue 7 https://doi.org/10.3390/biomedicines8070224	journal	July 2020
The Biochemical Role of the Human NEIL1 and NEIL3 DNA Glycosylases on Model DNA Replication Forks No authors listed Genes, Vol. 10, Issue 4 https://doi.org/10.3390/genes10040315	journal	April 2019
Organization of DNA in Mammalian Mitochondria Farge, Géraldine; Falkenberg, Maria International Journal of Molecular Sciences, Vol. 20, Issue 11 https://doi.org/10.3390/ijms20112770	journal	June 2019
NEIL1 and NEIL2 DNA glycosylases protect neural crest development against mitochondrial oxidative stress Han, Dandan; Schomacher, Lars; Schüle, Katrin M. eLife, Vol. 8 https://doi.org/10.7554/eLife.49044	journal	September 2019

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59 BASIC BIOLOGICAL SCIENCES
HDX-MS (hydrogen–deuterium exchange mass-spectrometry)
NEIL1 DNA glycosylase
base excision repair (BER)
mitochondrial transcription factor A (TFAM)
small angle X-ray scattering (SAXS)

Novel interaction interfaces mediate the interaction between the NEIL1 DNA glycosylase and mitochondrial transcription factor A

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References (89)

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