Search Results - "Prabu, J Rajan"

Interaction of Circadian Clock Proteins CRY1 and PER2 Is Modulated by Zinc Binding and Disulfide Bond Formation by Schmalen, Ira, Reischl, Silke, Wallach, Thomas, Klemz, Roman, Grudziecki, Astrid, Prabu, J. Rajan, Benda, Christian, Kramer, Achim, Wolf, Eva

“…Period (PER) proteins are essential components of the mammalian circadian clock. They form complexes with cryptochromes (CRY), which negatively regulate…”
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CUL5-ARIH2 E3-E3 ubiquitin ligase structure reveals cullin-specific NEDD8 activation by Kostrhon, Sebastian, Prabu, J. Rajan, Baek, Kheewoong, Horn-Ghetko, Daniel, von Gronau, Susanne, Klügel, Maren, Basquin, Jérôme, Alpi, Arno F., Schulman, Brenda A.

“…An emerging mechanism of ubiquitylation involves partnering of two distinct E3 ligases. In the best-characterized E3-E3 pathways, ARIH-family RING-between-RING…”
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Structure of the RNA Helicase MLE Reveals the Molecular Mechanisms for Uridine Specificity and RNA-ATP Coupling by Prabu, J. Rajan, Müller, Marisa, Thomae, Andreas W., Schüssler, Steffen, Bonneau, Fabien, Becker, Peter B., Conti, Elena

“…The MLE helicase remodels the roX lncRNAs, enabling the lncRNA-mediated assembly of the Drosophila dosage compensation complex. We identified a stable MLE core…”
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Interconversion between Anticipatory and Active GID E3 Ubiquitin Ligase Conformations via Metabolically Driven Substrate Receptor Assembly by Qiao, Shuai, Langlois, Christine R., Chrustowicz, Jakub, Sherpa, Dawafuti, Karayel, Ozge, Hansen, Fynn M., Beier, Viola, von Gronau, Susanne, Bollschweiler, Daniel, Schäfer, Tillman, Alpi, Arno F., Mann, Matthias, Prabu, J. Rajan, Schulman, Brenda A.

“…Cells respond to environmental changes by toggling metabolic pathways, preparing for homeostasis, and anticipating future stresses. For example, in…”
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Insights into the ISG15 transfer cascade by the UBE1L activating enzyme by Wallace, Iona, Baek, Kheewoong, Prabu, J. Rajan, Vollrath, Ronnald, von Gronau, Susanne, Schulman, Brenda A., Swatek, Kirby N.

“…The attachment of the ubiquitin-like protein ISG15 to substrates by specific E1-E2-E3 enzymes is a well-established signalling mechanism of the innate immune…”
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Structural insights into the nucleic acid remodeling mechanisms of the yeast THO-Sub2 complex by Schuller, Sandra K, Schuller, Jan M, Prabu, J Rajan, Baumgärtner, Marc, Bonneau, Fabien, Basquin, Jérôme, Conti, Elena

“…The yeast THO complex is recruited to active genes and interacts with the RNA-dependent ATPase Sub2 to facilitate the formation of mature export-competent…”
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Protein engineering of a ubiquitin-variant inhibitor of APC/C identifies a cryptic K48 ubiquitin chain binding site by Watson, Edmond R., Grace, Christy R. R., Zhang, Wei, Miller, Darcie J., Davidson, Iain F., Prabu, J. Rajan, Yu, Shanshan, Bolhuis, Derek L., Kulko, Elizaveta T., Vollrath, Ronnald, Haselbach, David, Stark, Holger, Peters, Jan-Michael, Brown, Nicholas G., Sidhu, Sachdev S., Schulman, Brenda A.

“…Ubiquitin (Ub)-mediated proteolysis is a fundamental mechanism used by eukaryotic cells to maintain homeostasis and protein quality, and to control timing in…”
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NEDD8 nucleates a multivalent cullin–RING–UBE2D ubiquitin ligation assembly by Baek, Kheewoong, Krist, David T., Prabu, J. Rajan, Hill, Spencer, Klügel, Maren, Neumaier, Lisa-Marie, von Gronau, Susanne, Kleiger, Gary, Schulman, Brenda A.

“…Eukaryotic cell biology depends on cullin–RING E3 ligase (CRL)-catalysed protein ubiquitylation 1 , which is tightly controlled by the modification of cullin…”
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Ubiquitin ligation to F-box protein targets by SCF–RBR E3–E3 super-assembly by Horn-Ghetko, Daniel, Krist, David T., Prabu, J. Rajan, Baek, Kheewoong, Mulder, Monique P. C., Klügel, Maren, Scott, Daniel C., Ovaa, Huib, Kleiger, Gary, Schulman, Brenda A.

“…E3 ligases are typically classified by hallmark domains such as RING and RBR, which are thought to specify unique catalytic mechanisms of ubiquitin transfer to…”
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Gene expression and cell identity controlled by anaphase-promoting complex by Oh, Eugene, Mark, Kevin G., Mocciaro, Annamaria, Watson, Edmond R., Prabu, J. Rajan, Cha, Denny D., Kampmann, Martin, Gamarra, Nathan, Zhou, Coral Y., Rape, Michael

“…Metazoan development requires the robust proliferation of progenitor cells, the identities of which are established by tightly controlled transcriptional…”
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Snapshots of RecA Protein Involving Movement of the C-domain and Different Conformations of the DNA-binding Loops: Crystallographic and Comparative Analysis of 11 Structures of Mycobacterium smegmatis RecA by Krishna, R., Prabu, J. Rajan, Manjunath, G.P., Datta, S., Chandra, N.R., Muniyappa, K., Vijayan, M.

“…Mycobacterium smegmatis RecA and its nucleotide complexes crystallize in three different, but closely related, forms characterized by specific ranges of unit…”
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GID E3 ligase supramolecular chelate assembly configures multipronged ubiquitin targeting of an oligomeric metabolic enzyme by Sherpa, Dawafuti, Chrustowicz, Jakub, Qiao, Shuai, Langlois, Christine R., Hehl, Laura A., Gottemukkala, Karthik Varma, Hansen, Fynn M., Karayel, Ozge, von Gronau, Susanne, Prabu, J. Rajan, Mann, Matthias, Alpi, Arno F., Schulman, Brenda A.

“…How are E3 ubiquitin ligases configured to match substrate quaternary structures? Here, by studying the yeast GID complex (mutation of which causes deficiency…”
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Mechanism of millisecond Lys48-linked poly-ubiquitin chain formation by cullin-RING ligases by Liwocha, Joanna, Li, Jerry, Purser, Nicholas, Rattanasopa, Chutima, Maiwald, Samuel, Krist, David T., Scott, Daniel C., Steigenberger, Barbara, Prabu, J. Rajan, Schulman, Brenda A., Kleiger, Gary

“…E3 ubiquitin ligases, in collaboration with E2 ubiquitin-conjugating enzymes, modify proteins with poly-ubiquitin chains. Cullin-RING ligase (CRL) E3s use…”
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Multifaceted N-Degron Recognition and Ubiquitylation by GID/CTLH E3 Ligases by Chrustowicz, Jakub, Sherpa, Dawafuti, Teyra, Joan, Loke, Mun Siong, Popowicz, Grzegorz M., Basquin, Jerome, Sattler, Michael, Prabu, J. Rajan, Sidhu, Sachdev S., Schulman, Brenda A.

“…[Display omitted] •Phage display identifies peptide motifs optimally binding GID/CTLH E3 ligases.•Substrate receptor loopsstructurally conform to diverse…”
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Structural snapshots along K48-linked ubiquitin chain formation by the HECT E3 UBR5 by Hehl, Laura A., Horn-Ghetko, Daniel, Prabu, J. Rajan, Vollrath, Ronnald, Vu, D. Tung, Pérez Berrocal, David A., Mulder, Monique P. C., van der Heden van Noort, Gerbrand J., Schulman, Brenda A.

“…Ubiquitin (Ub) chain formation by homologous to E6AP C-terminus (HECT)-family E3 ligases regulates vast biology, yet the structural mechanisms remain unknown…”
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Multisite phosphorylation dictates selective E2-E3 pairing as revealed by Ubc8/UBE2H-GID/CTLH assemblies by Chrustowicz, Jakub, Sherpa, Dawafuti, Li, Jerry, Langlois, Christine R, Papadopoulou, Eleftheria C, Vu, D Tung, Hehl, Laura A, Karayel, Özge, Beier, Viola, von Gronau, Susanne, Müller, Judith, Prabu, J Rajan, Mann, Matthias, Kleiger, Gary, Alpi, Arno F, Schulman, Brenda A

“…Ubiquitylation is catalyzed by coordinated actions of E3 and E2 enzymes. Molecular principles governing many important E3-E2 partnerships remain unknown,…”
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Noncanonical assembly, neddylation and chimeric cullin–RING/RBR ubiquitylation by the 1.8 MDa CUL9 E3 ligase complex by Horn-Ghetko, Daniel, Hopf, Linus V. M., Tripathi-Giesgen, Ishita, Du, Jiale, Kostrhon, Sebastian, Vu, D. Tung, Beier, Viola, Steigenberger, Barbara, Prabu, J. Rajan, Stier, Luca, Bruss, Elias M., Mann, Matthias, Xiong, Yue, Schulman, Brenda A.

“…Ubiquitin ligation is typically executed by hallmark E3 catalytic domains. Two such domains, ‘cullin–RING’ and ‘RBR’, are individually found in several hundred…”
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Structural studies on Mycobacterium tuberculosis RecA: Molecular plasticity and interspecies variability by Chandran, Anu V, Prabu, J Rajan, Nautiyal, Astha, Patil, K Neelakanteshwar, Muniyappa, K, Vijayan, M

“…Structures of crystals of Mycobacterium tuberculosis RecA, grown and analysed under different conditions, provide insights into hitherto underappreciated…”
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Crystallographic and modelling studies on Mycobacterium tuberculosis RuvA Additional role of RuvB-binding domain and inter species variability by Prabu, J Rajan, Thamotharan, S, Khanduja, Jasbeer Singh, Chandra, Nagasuma R, Muniyappa, K, Vijayan, M

“…RuvA, along with RuvB, is involved in branch migration of heteroduplex DNA in homologous recombination. The structures of three new crystal forms of RuvA from…”
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Functionally important movements in RecA molecules and filaments: studies involving mutation and environmental changes by Prabu, J. Rajan, Manjunath, G. P., Chandra, Nagasuma R., Muniyappa, K., Vijayan, M.

“…The crystal structures of mutants of Mycobacterium smegmatis RecA (MsRecA) involving changes of Gln196 from glutamine to alanine, asparagine and glutamic acid,…”
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