Article
Multidisciplinary Sciences
Lukas Schmauder, Klaus Richter
Summary: Nematode development is characterized by progression through several larval stages, with RNAi against hsp-90 and unc-45 causing arrest in development and affecting the behavior of specific gene coexpression cliques. By studying the behavior of these coexpression cliques, a better understanding of concerted responses at the genome-wide level in Caenorhabditis elegans can be achieved.
SCIENTIFIC REPORTS
(2021)
Article
Biochemistry & Molecular Biology
Taylor Moncrief, Courtney J. Matheny, Ivana Gaziova, John M. Miller, Hiroshi Qadota, Guy M. Benian, Andres F. Oberhauser
Summary: The proper folding and integration of myosin into thick filament structure depend on UNC-45/UNC-45B myosin chaperone molecules. Mutations in these molecules result in abnormal muscle function, likely due to reduced protein levels and chaperone activity. However, these mutations do not affect protein stability, suggesting a potential role of posttranslational modifications in protein instability.
Article
Fisheries
Yi-Li Gao, Asami Yoshida, Jin-Yang Liu, Takahiro Shimizu, Kazuya Shirota, Yasuhiko Shiina, Kiyoshi Osatomi
Summary: UNC-45B plays a crucial role in myosin assembly and the heat shock response in yellowtail. Short-term and long-term heat shock exposure resulted in significantly increased mRNA and protein expression levels of UNC-45B in yellowtail, especially during summer. The elevated expression levels of UNC-45B could potentially serve as a sensitive biomarker to predict heat shock resistance in aquaculture fish species, aiding in the selection of resilient juveniles for better production outcomes.
Article
Oncology
Xinliang Jiang, Junichi Maruyama, Hiroaki Iwasa, Kyoko Arimoto-Matsuzaki, Hiroshi Nishina, Yutaka Hata
Summary: YAP1, a co-transcription activator, serves as a thermosensor in response to heat shock conditions. Its subcellular localization is determined by phosphorylation status, with SRC and HSP90 involved in shuttling between the nucleus and cytoplasm. During heat shock, LATS2 forms aggregates and is dephosphorylated, influencing YAP1 activity in the cellular environment.
EXPERIMENTAL CELL RESEARCH
(2021)
Article
Food Science & Technology
Haotian Liu, Huan Zhang, Qian Liu, Qian Chen, Baohua Kong
Summary: This review highlights the importance and challenges of salt-soluble myofibrillar proteins and proposes strategies for inhibiting or disrupting the formation of myosin filaments. Key findings, such as the assembly mechanism of myosin filaments and the effects of chemical and physical strategies, are discussed, pointing out the limitations and the need for further research in achieving large-scale industrial production of novel meat protein based products.
TRENDS IN FOOD SCIENCE & TECHNOLOGY
(2021)
Article
Biophysics
Alma I. Plaza-Rodriguez, Ly T. S. Nguyen, Douglas N. Robinson, Pablo A. Iglesias
Summary: Cell shape change processes rely on a dynamic network of macromolecules which enable cells to sense and respond to mechanical cues. Myosin II and cortexillin I are critical elements of this cellular mechanosensory machinery and preassemble into complexes called contractility kits (CKs). Two IQGAP proteins differentially regulate the mechanoresponsiveness of the cortexillin I-myosin II elements within CKs. By developing a molecular model and conducting simulations, it was found that myosin II dimer formation dominates the temporal order of CK assembly and IQGAP proteins mediate cluster growth. Experimental validation confirmed the existence of ambiguous CKs that incorporate both classes of IQGAPs.
BIOPHYSICAL JOURNAL
(2022)
Article
Chemistry, Applied
Yanyun Zhang, Wenyan Fu, Dongmei Liu, Xing Chen, Peng Zhou
Summary: Enzymatic deamidation is a promising approach to improve the solubility of myofibrillar proteins in water. This study revealed that deamidation weakens the assembly ability of myosin thick filaments, and neutralizes positive charged clusters at a distance of 14-29 nm from the C-terminus, which impairs the ordered thick filament growth and promotes protein solubilization.
Article
Biochemistry & Molecular Biology
Zhuangzhuang Zhao, Ling-Dong Xu, Fei Zhang, Qi-Zhang Liang, Yajuan Jiao, Fang-Shu Shi, Biao He, Pinglong Xu, Yao-Wei Huang
Summary: Inhibition of heat shock protein 90 (Hsp90) effectively limits SARS-CoV-2 infection, but little is known about Hsp90 interaction with SARS-CoV-2 proteins. This study analyzed the effects of Hsp90 alpha and Hsp9011 on individual SARSCoV-2 viral proteins and found that five SARS-CoV-2 proteins are novel clients of Hsp9011. Hsp90 depletion-induced N protein degradation is independent of CHIP but alleviated by FBXO10.
JOURNAL OF BIOLOGICAL CHEMISTRY
(2023)
Article
Developmental Biology
Cody J. Drozd, Christopher C. Quinn
Summary: This study reveals the role of UNC-116/KIF5C and NEKL-3/NEK6/7 kinase in axon targeting in Caenorhabditis elegans. UNC-116 and UNC-16/JIP3 play important roles in axon termination, and NEKL-3 functions with RPM-1 ubiquitin ligase to promote axon termination.
Article
Chemistry, Applied
Ge Han, Jianhang Xu, Qian Chen, Xiufang Xia, Haotian Liu, Baohua Kong
Summary: This study investigated the effect of glycation on the solubility of myofibrillar proteins (MPs) in water. The results showed that MPs conjugated with dextran exhibited higher solubility and stability in water compared to other glycation products. The analysis suggested that the solubilization of MPs may be attributed to the changes in their secondary and tertiary structures.
Article
Biochemistry & Molecular Biology
Anuradhika Puri, Priyanka Singh, Navinder Kumar, Rajesh Kumar, Deepak Sharma
Summary: Prions are self-perpetuating infectious proteins. Tah1 is identified as a novel modulator of the yeast prion [URE3], influencing its formation and maintenance. The Hsp90 co-chaperone Tah1 is crucial for the assembly of small nucleolar ribonucleoprotein complexes.
JOURNAL OF MOLECULAR BIOLOGY
(2021)
Review
Biochemistry & Molecular Biology
Jeffrey Lynham, Walid A. Houry
Summary: Hsp90 is a ubiquitous molecular chaperone that plays an important role in cell signaling pathways. Its interactions with specific chaperones and cochaperones determine the folding of client proteins. Although it has multiple roles in protein complex assembly, the detailed mechanisms are still not fully understood.
Article
Agriculture, Multidisciplinary
Tian Fang, Mengfan Han, Yue Wang, Xiaomei Xiang, Lin Chen, Huijuan Yang, Zhuangli Kang, Feng Huang, Xiaojing Fan, Minyi Han, Xinglian Xu, Guanghong Zhou, Niamat Ullah, Xianchao Feng
Summary: This study investigated the effects of different heating rates on the self-assembly behavior, physicochemical properties, structure, and gelling properties of myosin. It was found that the lowest heating rate of 1°C/min resulted in a denser microstructure, the highest elastic modulus, and water holding capacity in the myosin gel. Additionally, the lower heating rate allowed for sufficient denaturation and full structure unfolding of myosin, leading to the formation of regular and homogeneous spherical aggregates and a better three-dimensional network in the myosin gel.
JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE
(2023)
Article
Multidisciplinary Sciences
Dimitra Keramisanou, M. V. Vasantha Kumar, Nicole Boose, Rinat R. Abzalimov, Ioannis Gelis
Summary: This study investigates the recruitment and loading mechanism of protein kinases to the Hsp90-Cdc37 complex, which is the first step in Hsp90-mediated chaperoning. The results show that the conformational dynamics of all partners are critical for the loading mechanism, and that Cdc37 plays a role in sensing clients by stabilizing the preexisting partially unfolded client state. These findings reveal the regulatory mechanism of molecular chaperones in maintaining protein homeostasis.
Article
Multidisciplinary Sciences
Benoit Bragantini, Christophe Charron, Maxime Bourguet, Arnaud Paul, Decebal Tiotiu, Benjamin Rothe, Helene Marty, Guillaume Terral, Steve Hessmann, Laurence Decourty, Marie-Eve Chagot, Jean-Marc Strub, Severine Massenet, Edouard Bertrand, Marc Quinternet, Cosmin Saveanu, Sarah Cianferani, Stephane Labialle, Xavier Manival, Bruno Charpentier
Summary: Biogenesis of eukaryotic box C/D small nucleolar ribonucleoproteins involves various assembly machinery components and genetic interactions with chromatin organization factors. Bcd1p regulates the recruitment of histone chaperone Rtt106p by modulating its association with RNA polymerase II and levels of H3K56ac. The study provides evidence for a protein interaction interface for Rtt106p that controls its transcription-associated activity, and suggests a link between ribosome formation and chromatin functions.
NATURE COMMUNICATIONS
(2021)