A5067273906- S100 Proteins and Annexins
- Cardiomyopathy and Myosin Studies
- Protein Structure and Dynamics
- Muscle Physiology and Disorders
- Cellular Mechanics and Interactions
- Protease and Inhibitor Mechanisms
- Microtubule and mitosis dynamics
- Machine Learning in Bioinformatics
- Enzyme Structure and Function
- RNA and protein synthesis mechanisms
- Computational Drug Discovery Methods
- Peptidase Inhibition and Analysis
- Cell Adhesion Molecules Research
- Hippo pathway signaling and YAP/TAZ
- Ion channel regulation and function
- Slime Mold and Myxomycetes Research
- RNA Research and Splicing
- Antimicrobial Peptides and Activities
- Chemical Synthesis and Analysis
- Photosynthetic Processes and Mechanisms
- Ubiquitin and proteasome pathways
- Diatoms and Algae Research
- Advanced Proteomics Techniques and Applications
- Protein Kinase Regulation and GTPase Signaling
- Advanced Fluorescence Microscopy Techniques
Eötvös Loránd University
2015-2024
Pázmány Péter Catholic University
2005-2018
University of Copenhagen
2012
National Institutes of Health
2004
National Heart Lung and Blood Institute
2004
Brandeis University
1990-1991
Abstract A few highly charged natural peptide sequences were recently suggested to form stable α‐helical structures in water. In this article we show that these represent a novel structural motif called “charged single α‐helix” (CSAH). To obtain reliable candidate CSAH motifs, developed two conceptually different computational methods capable of scanning large databases: SCAN4CSAH is based on sequence features characteristic for salt bridge stabilized α‐helices, whereas FT_CHARGE applies...
LC8 dynein light chain (DYNLL) is a eukaryotic hub protein that thought to function as dimerization engine. Its interacting partners are involved in wide range of cellular functions. In its dozens hitherto identified binding DYNLL binds linear peptide segment. The known segments define loosely characterized motif: [D/S]-4K-3X-2[T/V/I]-1Q0[T/V]1[D/E]2. motifs localized disordered the DYNLL-binding proteins and often flanked by coiled coil or other potential domains. Based on directed...
S100A4 is a member of the S100 family calcium-binding proteins that directly involved in tumor metastasis. It binds to nonmuscle myosin IIA (NMIIA) tail near assembly competence domain (ACD) promoting filament disassembly, which could be associated with increasing metastatic potential cells. Here, we investigate mechanism S100A4–NMIIA interaction based on binding studies and crystal structure complex 45-residue-long heavy chain fragment. Interestingly, also find as strongly homologous...
Light meromyosin (LMM), prepared by limited tryptic digestion of myosin, usually contains several polypeptide chains, LMM-A, LMM-B, and LMM-C in decreasing order molecular weight estimated from sodium dodecyl sulfate-gel electrophoresis. Further LMM produces well defined fragments (Balint, M., Szilagyi, L., Fekete, Gy., Blazso, Biro, E. N. A. J. Mol. Biol. (1968) 37, 317-330). Fragments LF-1, LMM-D, LF-2, LF-3, with chain masses equal to 63, 56, 47, 30 kDa, respectively, have been isolated...
Abstract The 20 residue long Trp‐cage is the smallest protein known, and thus has been subject of several in vitro silico folding studies. Here, we report multistate scenario miniprotein atomic detail. We detected characterized different intermediate states by temperature dependent NMR measurements 15 N 13 C/ labeled protein, both at neutral acidic pH values. developed a deconvolution technique to characterize invisible—fully folded, unfolded intermediate—fast exchanging states. Using...
The calcium‐binding, vertebrate‐specific S100 protein family consists of 20 paralogs in humans (referred as the S100ome), with several clinically important members. To explore their protein–protein interactions (PPIs) quantitatively, we have chosen an unbiased, high‐throughput, competitive fluorescence polarization (FP) assay that revealed a partial functional redundancy when complete S100ome ( n = 20) was tested against numerous model partners 13). Based on specificity, can be grouped into...
The regulatory domain of scallop myosin, consisting a light chain (R-LC), an essential (E-LC), and portion heavy chain, occupies the neck region myosin. This is directly involved in regulation molluscan muscle contraction, which triggered by direct Ca2+ binding to We have isolated soluble functional complex (regulatory complex) comprised R-LC, E-LC, 10-kDa fragment 1:1:1 stoichiometry clostripain digestion myosin head (papain subfragment 1). N termini fragments were either leucine-812 or...
A 10 kDa dynein light chain (DLC), previously identified as a tail of myosin Va, may function cargo-binding and/or regulatory subunit both and dynein. Here, we identify characterize the binding site DLC on Va. Fragments human Va DLC2 isoform were expressed, their complex formation was analyzed by pull-down assays, gel filtration, spectroscopic methods. found to bind homodimer ∼15 residue segment (Ile1280−Ile1294) localized between medial distal coiled-coil domains tail. The region contains...
Assembly and disassembly of protein-protein complexes needs to be dynamically controlled phosphoswitches based on linear motifs are crucial in this process. Extracellular signal-regulated kinase 2 (ERK2) recognizes a linear-binding motif at the C-terminal tail (CTT) ribosomal S6 1 (RSK1), leading phosphorylation subsequent activation RSK1. The CTT also contains classical PDZ domain-binding which binds RSK substrates (e.g. MAGI-1). We show that autophosphorylation disordered promotes...
We have determined the primary structure of myosin heavy chain (MHC) striated adductor muscle scallop Aequipecten irradians by cloning and sequencing its cDNA. It is first sequence obtained in a directly Ca(2+)-regulated myosin. The 1938-amino acid has an overall similar to other MHCs. subfragment-1 region MHC 59-62% identity with sarcomeric 52-53% nonsarcomeric (smooth metazoan nonmuscle) component regulatory domain (Kwon, H., Goodwin, E. B., Nyitray, L., Berliner, E., O'Neall-Hennessey,...
Myosin V is the best characterized vesicle transporter in vertebrates, but it has been unknown as to whether all members of myosin family share a common, evolutionarily conserved mechanism action. Here we show that from Drosophila strikingly different motor vertebrate Va, and nonprocessive, ensemble motor. Our steady-state transient kinetic measurements on single-headed constructs reveal single molecule spends most its mechanochemical cycle time detached actin, therefore function processive...
We report here that the catch and striated adductor muscle myosin heavy-chain (MHC) isoforms of scallop (Argopecten irradians, previously Aequipecten irradians) are generated by alternative RNA splicing from a single gene. Scallop cDNA genomic DNA were amplified PCR using primers based on sequenced MHC cDNA. Mapping exon/intron borders sequencing full-length in overlapping fragments revealed 24-kb gene encodes polypeptide 27 exons four sets tandem exon pairs alternatively spliced into...