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Maher, L. James

Mayo Clinic

Mayo Clinic

Citations 27

Author response: Unexpected sequences and structures of mtDNA required for efficient transcription from the first heavy-strand promoter
Uchida, Akira , Murugesapillai, Divakaran , Wang, Yao , Lodeiro, María F. , Prabhakar, Shaan, Oliver, Guinevere V , Arnold, Jamie J. , Maher, L. James, Cameron, Craig E. , Kastner, Markus , Williams, Mark C.

No container title available | August 10, 2017 | Volume: No volume available | Issue: No issue available | Pages: No page available

10.7554/elife.27283.032 Get It

Accurate nanoscale flexibility measurement of DNA and DNA–protein complexes by atomic force microscopy in liquid
Murugesapillai, Divakaran , Bouaziz, Serge , Maher, L. James, Israeloff, Nathan, Cameron, Craig E. , Williams, Mark C. , Williams, Mark C

Nanoscale | August 1, 2017 | Volume: 9 | Issue: 31 | Pages: 11327-11337

10.1039/c7nr04231k Get It

We obtain accurate three-dimensional persistence length measurements for DNA and DNA–protein complexes using liquid AFM imaging, validated by optical tweezers.
Unexpected sequences and structures of mtDNA required for efficient transcription from the first heavy-strand promoter
Uchida, Akira , Murugesapillai, Divakaran , Kastner, Markus , Lodeiro, María F. , Prabhakar, Shaan, Oliver, Guinevere V , Arnold, Jamie J. , Maher, L. James, Williams, Mark C. , Cameron, Craig E. , Oliver, Guinevere V , Arnold, Jamie J , Williams, Mark C , Cameron, Craig E , Wang, Yao

eLife | July 26, 2017 | Volume: 6 | Issue: No issue available | Pages: No page available

10.7554/elife.27283 Get It

Human mtDNA contains three promoters, suggesting a need for differential expression of the mitochondrial genome. Studies of mitochondrial transcription have used a reductionist approach, perhaps masking differential regulation. Here we evaluate transcription from light-strand (LSP) and heavy-strand (HSP1) promoters using templates that mimic their natural context. These studies reveal sequences upstream, hypervariable in the human population (HVR3), and downstream of the HSP1 transcription start site required for maximal yield. The carboxy-terminal tail of TFAM is essential for activation of HSP1 but not LSP. Images of the template obtained by atomic force microscopy show that TFAM creates loops in a discrete region, the formation of which correlates with activation of HSP1; looping is lost in tail-deleted TFAM. Identification of HVR3 as a transcriptional regulatory element may contribute to between-individual variability in mitochondrial gene expression. The unique requirement of HSP1 for the TFAM tail may enable its regulation by post-translational modifications.
Cyclin A2 is an RNA binding protein that controls Mre11 mRNA translation
Jeganathan, Karthik B. , Limzerwala, Jazeel F. , Baker, Darren J. , Hamada, Masakazu , Nam, Hyun-Ja, Deursen, Willemijn H. van , Hamada, Naomi, Naylor, Ryan M. , Becker, Nicole A. , Davies, Brian A., Ree, Janine H. van, Mer, Georges , Maher, L. James, Katzmann, David J. , Deursen, Jan M. van , Kanakkanthara, Arun , van Deursen, Willemijn H, van Ree, Janine H, Shapiro, Virginia S, Hamada, Masakazu, Shapiro, Virginia Smith , Jeganathan, Karthik B , Baker, Darren J

Science | September 29, 2016 | Volume: 353 | Issue: 6307 | Pages: 1549-1552

10.1126/science.aaf7463 Get It

Cyclin A2 activates the cyclin-dependent kinases Cdk1 and Cdk2 and is expressed at elevated levels from S phase until early mitosis. We found that mutant mice that cannot elevate cyclin A2 are chromosomally unstable and tumor-prone. Underlying the chromosomal instability is a failure to up-regulate the meiotic recombination 11 (Mre11) nuclease in S phase, which leads to impaired resolution of stalled replication forks, insufficient repair of double-stranded DNA breaks, and improper segregation of sister chromosomes. Unexpectedly, cyclin A2 controlled Mre11 abundance through a C-terminal RNA binding domain that selectively and directly binds Mre11 transcripts to mediate polysome loading and translation. These data reveal cyclin A2 as a mechanistically diverse regulator of DNA replication combining multifaceted kinase-dependent functions with a kinase-independent, RNA binding–dependent role that ensures adequate repair of common replication errors.
Anti-Transcription Factor RNA Aptamers as Potential Therapeutics
Mondragón, Estefanía, Maher, L. James, Maher, Louis James

Nucleic Acid Therapeutics | October 28, 2015 | Volume: 26 | Issue: 1 | Pages: 29-43

10.1089/nat.2015.0566 Get It

Transcription factors (TFs) are DNA-binding proteins that play critical roles in regulating gene expression. These proteins control all major cellular processes, including growth, development, and homeostasis. Because of their pivotal role, cells depend on proper TF function. It is, therefore, not surprising that TF deregulation is linked to disease. The therapeutic drug targeting of TFs has been proposed as a frontier in medicine. RNA aptamers make interesting candidates for TF modulation because of their unique characteristics. The products of in vitro selection, aptamers are short nucleic acids (DNA or RNA) that bind their targets with high affinity and specificity. Aptamers can be expressed on demand from transgenes and are intrinsically amenable to recognition by nucleic acid-binding proteins such as TFs. In this study, we review several natural prokaryotic and eukaryotic examples of RNAs that modulate the activity of TFs. These examples include 5S RNA, 6S RNA, 7SK, hepatitis delta virus-RNA (HDV-RNA), neuron restrictive silencer element (NRSE)-RNA, growth arrest-specific 5 (Gas5), steroid receptor RNA activator (SRA), trophoblast STAT utron (TSU), the 3′ untranslated region of caudal mRNA, and heat shock RNA-1 (HSR1). We then review examples of unnatural RNA aptamers selected to inhibit TFs nuclear factor-kappaB (NF-κB), TATA-binding protein (TBP), heat shock factor 1 (HSF1), and runt-related transcription factor 1 (RUNX1). The field of RNA aptamers for DNA-binding proteins continues to show promise.
Modeling dioxygenase enzyme kinetics in familial paraganglioma
Peters, Justin P. , Her, Yeng F., Maher, L. James

Biology Open | September 15, 2015 | Volume: 4 | Issue: 10 | Pages: 1281-1289

10.1242/bio.013623 Get It

ABSTRACT Hypoxia inducible factors (HIFs) play vital roles in cellular maintenance of oxygen homeostasis. These transcription factors are responsible for the expression of genes involved in angiogenesis, metabolism, and cell proliferation. Here, we generate a detailed mathematical model for the enzyme kinetics of α-ketoglutarate-dependent HIF prolyl 4-hydroxylase domain (PHD) dioxygenases to simulate our in vitro data showing synergistic PHD inhibition by succinate and hypoxia in experimental models of succinate dehydrogenase loss, which phenocopy familial paraganglioma. Our mathematical model confirms the inhibitory synergy of succinate and hypoxia under physiologically-relevant conditions. In agreement with our experimental data, the model predicts that HIF1α is not stabilized under atmospheric oxygen concentrations, as observed. Further, the model confirms that addition of α-ketoglutarate can reverse PHD inhibition by succinate and hypoxia in SDH-deficient cells.
Succinate Dehydrogenase Loss in Familial Paraganglioma: Biochemistry, Genetics, and Epigenetics
Her, Yeng F., Maher, L. James

International Journal of Endocrinology | July 29, 2015 | Volume: 2015 | Issue: No issue available | Pages: 1-14

10.1155/2015/296167 Get It

It is counterintuitive that metabolic defects reducing ATP production can cause, rather than protect from, cancer. Yet this is precisely the case for familial paraganglioma, a form of neuroendocrine malignancy caused by loss of succinate dehydrogenase in the tricarboxylic acid cycle. Here we review biochemical, genetic, and epigenetic considerations in succinate dehydrogenase loss and present leading models and mysteries associated with this fascinating and important tumor.
High-resolution mapping of architectural DNA binding protein facilitation of a DNA repression loop in Escherichia coli
Becker, Nicole A. , Maher, L. James

Proceedings of the National Academy of Sciences | May 27, 2015 | Volume: 112 | Issue: 23 | Pages: 7177-7182

10.1073/pnas.1500412112 Get It

Significance Double-stranded DNA is one of the stiffest polymers in biology, resisting both bending and twisting over hundreds of base pairs. However, tightly bent DNA loops are formed by proteins that turn off (repress) genes in bacteria. It has been shown that “architectural” proteins capable of kinking any DNA molecule without sequence preference facilitate this kind of gene repression. The mechanism of this effect is unknown for DNA loops involving the well-known Escherichia coli lac repressor. Here we adapt high-resolution protein-mapping techniques to show that an architectural protein directly binds tightly looped DNA to facilitate gene repression by the lac repressor.
Quantitative PCR Analysis of DNA Aptamer Pharmacokinetics in Mice
Perschbacher, Katherine J , Smestad, John , Peters, Justin P. , Standiford, Miranda M., Đenić, Aleksandar , Wootla, Bharath , Warrington, Arthur E. , Rodriguez, Moses , Maher, L. James, Perschbacher, Katherine, Wootla, Bharath , Denic, Aleksandar , Rodriguez, Moses , Smestad, John

Nucleic Acid Therapeutics | December 23, 2014 | Volume: 25 | Issue: 1 | Pages: 11-19

10.1089/nat.2014.0515 Get It

DNA aptamer oligonucleotides and their protein conjugates show promise as therapeutics in animal models of diseases such as multiple sclerosis. These molecules are large and highly charged, raising questions about their biodistribution and pharmacokinetics in mammals. Here we exploit the power of quantitative polymerase chain reaction to accurately quantitate the tissue distribution of 40-nucleotide DNA aptamers and their streptavidin conjugates after intraperitoneal injection in mice. We show remarkably rapid distribution to peripheral tissues including the central nervous system. Modeling of tissue distribution data reveals the importance of DNA aptamer sequence, 3′ modification, and protein conjugation in enhancing tissue exposure. These data help to interpret the previously observed effectiveness of aptamer conjugates, as opposed to free aptamers, in stimulating central nervous system remyelination in a mouse model of multiple sclerosis.
The free solution mobility of DNA and other analytes varies as the logarithm of the fractional negative charge
Stellwagen, Nancy C. , Peters, Justin P. , Dong, Qian , Maher, L. James, Stellwagen, Earle

ELECTROPHORESIS | March 20, 2014 | Volume: 35 | Issue: 12-13 | Pages: 1855-1863

10.1002/elps.201400040 Get It

The free solution mobilities of ssDNA and dsDNA molecules with variable charge densities have been measured by CE. DNA charge density was modified either by appending positively or negatively charged groups to the thymine residues in a 98 bp DNA molecule, or by replacing some of the negatively charged phosphate internucleoside linkers in small ssDNA or dsDNA oligomers with positively charged phosphoramidate linkers. Mobility ratios were calculated for each dataset by dividing the mobility of a charge variant by the mobility of its unmodified parent DNA. Mobility ratios essentially eliminate the effect of the BGE on the observed mobility, making it possible to compare analytes measured under different experimental conditions. Neutral moieties attached to the thymine residues in the 98‐bp DNA molecule had little or no effect on the mobility ratios, indicating that bulky substituents in the DNA major groove do not affect the mobility significantly. The mobility ratios observed for the thymine‐modified and linker‐modified DNA charge variants increased approximately linearly with the logarithm of the fractional negative charge of the DNA. Mobility ratios calculated from previous studies of linker‐modified DNA charge variants and small multicharged organic molecules also increased approximately linearly with the logarithm of the fractional negative charge of the analyte. The results do not agree with the Debye–Hückel–Onsager theory of electrophoresis, which predicts that the mobility of an analyte should depend linearly on analyte charge, not the logarithm of the charge, when the frictional coefficient is held constant.