Michael L. Nosella

The Expanding Histone Universe: Histone-Based DNA Organization in Noneukaryotic Organisms

Alejandro Villalta, Sashi R. Weerawarana, Michael L. Nosella, Karolin Luger

Histones are small basic proteins that form the proteinaceous core of the nucleosome, the repeating building block of chromatin in all eukaryotes. Long thought to be exclusive to eukaryotes, histones are now increasingly appreciated for their roles in organizing genomes across all …

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The dynamic and heterogeneous composition of biomolecular condensates and its functional relevance

Christopher Chin Sang, Sayantani Upadhyay, Michael L. Nosella, Julie D. Forman‐Kay et autres

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Modulation of histone tail electrostatic potentials in nucleosome core particles by acetylation and PARylation

Nicolas Bolik-Coulon, Philip Rößler, Michael L. Nosella, Tae Hun Kim et autres

Cellular DNA is wrapped about an octamer composed of four histone proteins forming the fundamental unit of chromatin structure, the nucleosome core particle (NCP). The intrinsically disordered tails of the histones serve as scaffolds for binding an array of proteins that regulate …

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PARP1 condensates differentially partition DNA repair proteins and enhance DNA ligation

Christopher Chin Sang, Gaelen Moore, Maria Tereshchenko, Hongshan Zhang et autres

Poly(ADP-ribose) polymerase 1 (PARP1) is one of the first responders to DNA damage and plays crucial roles in recruiting DNA repair proteins through its activity - poly(ADP-ribosyl)ation (PARylation). The enrichment of DNA repair proteins at sites of DNA damage has been described …

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Chromosome compaction is triggered by an autonomous DNA-binding module within condensin

Alyssa Pastic, Michael L. Nosella, Annahat Kochhar, Zi Hao Liu et autres

The compaction of chromatin into mitotic chromosomes is essential for faithful transmission of the genome during cell division. In eukaryotes, chromosome morphogenesis is regulated by the condensin complex, though the exact mechanism used to target condensin to chromatin and initiate condensation is …

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Author Reply to Peer Reviews of PARP1 condensates differentially partition DNA repair proteins and enhance DNA ligation

Christopher Chin Sang, Gaelen Moore, Maria Tereshchenko, Hongshan Zhang et autres

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PARP1 condensates differentially partition DNA repair proteins and enhance DNA ligation

Christopher Chin Sang, Gaelen Moore, Maria Tereshchenko, Michael L. Nosella et autres

ABSTRACT Poly(ADP-ribose) polymerase 1 (PARP1) is one of the first responders to DNA damage and plays crucial roles in recruiting DNA repair proteins through its activity – poly(ADP-ribosyl)ation (PARylation). The enrichment of DNA repair proteins at sites of DNA damage has been …

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Poly(ADP-ribosyl)ation enhances nucleosome dynamics and organizes DNA damage repair components within biomolecular condensates

Michael L. Nosella, Tae Hun Kim, Shuya Kate Huang, Robert W. Harkness et autres

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Exploration of O-GlcNAc transferase glycosylation sites reveals a target sequence compositional bias

P. Andrew Chong, Michael L. Nosella, Manasvi Vanama, Roxana Ruiz-Arduengo et autres

O-GlcNAc transferase (OGT) is an essential glycosylating enzyme that catalyzes the addition of N-acetylglucosamine to serine or threonine residues of nuclear and cytoplasmic proteins. The enzyme glycosylates a broad range of peptide sequences and the prediction of glycosylation sites has proven challenging. …

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Correlating histone acetylation with nucleosome core particle dynamics and function

Tae Hun Kim, Michael L. Nosella, Nicolas Bolik-Coulon, Robert W. Harkness et autres

Epigenetic modifications of chromatin play a critical role in regulating the fidelity of the genetic code and in controlling the translation of genetic information into the protein components of the cell. One key posttranslational modification is acetylation of histone lysine residues. Molecular …

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Exploration of O-GlcNAc-transferase (OGT) glycosylation sites reveals a target sequence compositional bias

P. Andrew Chong, Michael L. Nosella, Manasvi Vanama, Roxana Ruiz-Arduengo et autres

Abstract O-GlcNAc transferase (OGT) is an essential glycosylating enzyme that catalyzes the addition of N-acetylglucosamine to serine or threonine residues of nuclear and cytoplasmic proteins. The enzyme glycosylates a broad range of peptide sequences and prediction of glycosylation sites has proven challenging. …

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DATA for Exploration of O-GlcNAc-transferase (OGT) glycosylation sites reveals a target sequence compositional bias

P. Andrew Chong, Michael L. Nosella, Manasvi Vanama, Roxana Ruiz-Arduengo et autres

Mass spectrometry data for identification of glycosylation sites in CBP ID3 and EWS LCRn Perl based implementation of glycosylation Site Predictor OGTcomPred

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