keyword
MENU ▼
Read by QxMD icon Read
search

Protein chaperones

keyword
https://www.readbyqxmd.com/read/27920299/the-type-iii-secretion-system-effector-sptp-of-salmonella-enterica-serovar-typhi
#1
Rebecca Johnson, Alexander Byrne, Cedric N Berger, Elizabeth Klemm, Valerie F Crepin, Gordon Dougan, Gad Frankel
: Salmonella enterica serovars causes gastroenteritis or typhoid fever in humans, with virulence depending on the action of two type III secretion systems (SPI-1 and SPI-2). SptP is a Salmonella SPI-1 effector, involved in mediating recovery of the host cytoskeleton post-infection. SptP requires a chaperone, SicP, for stability and secretion. SptP has 94% identity between S Typhimurium and S Typhi; direct comparison of the protein sequences revealed that S Typhi SptP has numerous amino acid changes within its chaperone-binding domain...
December 5, 2016: Journal of Bacteriology
https://www.readbyqxmd.com/read/27918543/ficd-acts-bifunctionally-to-ampylate-and-de-ampylate-the-endoplasmic-reticulum-chaperone-bip
#2
Steffen Preissler, Claudia Rato, Luke A Perera, Vladimir Saudek, David Ron
Protein folding homeostasis in the endoplasmic reticulum (ER) is defended by an unfolded protein response that matches ER chaperone capacity to the burden of unfolded proteins. As levels of unfolded proteins decline, a metazoan-specific FIC-domain-containing ER-localized enzyme (FICD) rapidly inactivates the major ER chaperone BiP by AMPylating T518. Here we show that the single catalytic domain of FICD can also release the attached AMP, restoring functionality to BiP. Consistent with a role for endogenous FICD in de-AMPylating BiP, FICD(-/-) hamster cells are hypersensitive to introduction of a constitutively AMPylating, de-AMPylation-defective mutant FICD...
December 5, 2016: Nature Structural & Molecular Biology
https://www.readbyqxmd.com/read/27917864/multivalent-contacts-of-the-hsp70-ssb-contribute-to-its-architecture-on-ribosomes-and-nascent-chain-interaction
#3
Marie A Hanebuth, Roman Kityk, Sandra J Fries, Alok Jain, Allison Kriel, Veronique Albanese, Tancred Frickey, Christine Peter, Matthias P Mayer, Judith Frydman, Elke Deuerling
Hsp70 chaperones assist de novo folding of newly synthesized proteins in all cells. In yeast, the specialized Hsp70 Ssb directly binds to ribosomes. The structural basis and functional mode of recruitment of Ssb to ribosomes is not understood. Here, we present the molecular details underlying ribosome binding of Ssb in Saccharomyces cerevisiae. This interaction is multifaceted, involving the co-chaperone RAC and two specific regions within Ssb characterized by positive charges. The C-terminus of Ssb mediates the key contact and a second attachment point is provided by a KRR-motif in the substrate binding domain...
December 5, 2016: Nature Communications
https://www.readbyqxmd.com/read/27917829/the-er-stress-sensor-perk-luminal-domain-functions-as-a-molecular-chaperone-to-interact-with-misfolded-proteins
#4
Peng Wang, Jingzhi Li, Bingdong Sha
PERK is one of the major sensor proteins which can detect the protein-folding imbalance generated by endoplasmic reticulum (ER) stress. It remains unclear how the sensor protein PERK is activated by ER stress. It has been demonstrated that the PERK luminal domain can recognize and selectively interact with misfolded proteins but not native proteins. Moreover, the PERK luminal domain may function as a molecular chaperone to directly bind to and suppress the aggregation of a number of misfolded model proteins...
December 1, 2016: Acta Crystallographica. Section D, Structural Biology
https://www.readbyqxmd.com/read/27916943/the-large-phenotypic-spectrum-of-fabry-disease-requires-graduated-diagnosis-and-personalized-therapy-a-meta-analysis-can-help-to-differentiate-missense-mutations
#5
Valentina Citro, Marco Cammisa, Ludovica Liguori, Chiara Cimmaruta, Jan Lukas, Maria Vittoria Cubellis, Giuseppina Andreotti
Fabry disease is caused by mutations in the GLA gene and is characterized by a large genotypic and phenotypic spectrum. Missense mutations pose a special problem for graduating diagnosis and choosing a cost-effective therapy. Some mutants retain enzymatic activity, but are less stable than the wild type protein. These mutants can be stabilized by small molecules which are defined as pharmacological chaperones. The first chaperone to reach clinical trial is 1-deoxygalactonojirimycin, but others have been tested in vitro...
December 1, 2016: International Journal of Molecular Sciences
https://www.readbyqxmd.com/read/27916661/tetrameric-assembly-of-k-channels-requires-er-located-chaperone-proteins
#6
Kai Li, Qiang Jiang, Xue Bai, Yi-Feng Yang, Mei-Yu Ruan, Shi-Qing Cai
Tetrameric assembly of channel subunits in the endoplasmic reticulum (ER) is essential for surface expression and function of K(+) channels, but the molecular mechanism underlying this process remains unclear. In this study, we found through genetic screening that ER-located J-domain-containing chaperone proteins (J-proteins) are critical for the biogenesis and physiological function of ether-a-go-go-related gene (ERG) K(+) channels in both Caenorhabditis elegans and human cells. Human J-proteins DNAJB12 and DNAJB14 promoted tetrameric assembly of ERG (and Kv4...
November 30, 2016: Molecular Cell
https://www.readbyqxmd.com/read/27914074/common-challenges-in-studying-the-structure-and-function-of-bacterial-proteins-case-studies-from-helicobacter-pylori
#7
Daniel A Bonsor, Eric J Sundberg
Employing biophysical and structural methods is a powerful way to elucidate mechanisms of molecular recognition in bacterial pathogenesis. Such studies invariably depend on the production of pure, folded and stable proteins. Many proteins that can be expressed recombinantly ultimately fail to meet one or more of these criteria. The cag proteins from Helicobacter pylori form a secretion system that delivers the oncoprotein, CagA, into human gastric epithelial cells through an interaction between CagL and host cell integrins, where it can cause gastric adenocarcinoma...
2017: Methods in Molecular Biology
https://www.readbyqxmd.com/read/27913624/bcp1-is-the-nuclear-chaperone-of-the-60s-ribosomal-protein-rpl23-in-saccharomyces-cerevisiae
#8
Ya-Han Ting, Ting-Jun Lu, Arlen W Johnson, Jing-Ting Shie, Bo-Ru Chen, Suresh Kumar S, Kai-Yin Lo
Eukaryotic ribosomes are composed of rRNAs and ribosomal proteins. Ribosomal proteins are translated in the cytoplasm and imported into the nucleus for assembly with the rRNAs. It has been shown that chaperones or karyopherins responsible for import can maintain the stability of ribosomal proteins by neutralizing unfavorable positive charges and thus facilitate their transports. Among 79 ribosomal proteins in yeast, only few are identified with specific chaperones. Besides the classic role in maintaining protein stability, chaperones have additional roles in transport, chaperoning the assembly site, and dissociation of ribosomal proteins from karyopherins...
December 2, 2016: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/27913182/virtual-screening-and-biophysical-studies-lead-to-hsp90-inhibitors
#9
Renjie Huang, Daniel M Ayine-Tora, M Nasri Muhammad Rosdi, Yu Li, Jóhannes Reynisson, Ivanhoe K H Leung
Heat shock protein 90 (HSP90) is a molecular chaperone that plays important functional roles in cells. The chaperone activity of HSP90 is regulated by the hydrolysis of ATP at the protein's N-terminal domain. HSP90, in particular the N-terminal domain, is a current inhibition target for therapeutic treatments of cancers. This paper describes an application of virtual screening, thermal shift assaying and protein NMR spectroscopy leading to the discovery of HSP90 inhibitors that contain the resorcinol structure...
November 23, 2016: Bioorganic & Medicinal Chemistry Letters
https://www.readbyqxmd.com/read/27911725/the-multiple-roles-of-the-nucleocapsid-in-retroviral-rna-conversion-into-proviral-dna-by-reverse-transcriptase
#10
REVIEW
Jean-Luc Darlix, Hugues de Rocquigny, Yves Mély
Retroviruses are enveloped plus-strand RNA viruses that can cause cancer, immunodeficiency and neurological disorder in human and animals. Retroviruses have several unique properties, such as a genomic RNA in a dimeric form found in the virus, and a replication strategy called 'copy-and-paste' during which the plus-strand genomic RNA is converted into a double-stranded DNA, subsequently integrated into the cellular genome. Two essential viral enzymes, reverse transcriptase (RT) and integrase (IN), direct this 'copy-and-paste' replication...
October 15, 2016: Biochemical Society Transactions
https://www.readbyqxmd.com/read/27909750/repression-of-proteases-and-hsp90-chaperone-expression-induced-by-an-antiretroviral-in-virulent-environmental-strains-of-cryptococcus-neoformans
#11
Cleber Fernando Serafin, Ana Paula Paris, Claudete Rodrigues Paula, Rita Cássia Garcia Simão, Rinaldo Ferreira Gandra
This study evaluated the effect of the antiretroviral ritonavir on protease secretion in different strains of Cryptococcus neoformans isolated from the environment and investigated the expression of heat shock protein (Hsp90), classically described virulence factors in other yeast in the presence of the same antiretroviral. The presence of the enzyme was detected by the formation of a degradation of the halo around the colonies. The results were classified as follows: level 1 (without proteases), level 2 (positive for proteases), and level 3 (strongly positive for proteases)...
December 2, 2016: Microbial Ecology
https://www.readbyqxmd.com/read/27909051/the-chaperone-activity-and-substrate-spectrum-of-human-small-heat-shock-proteins
#12
Evgeny V Mymrikov, Marina Daake, Bettina Richter, Martin Haslbeck, Johannes Buchner
Small heat shock proteins (sHsps) are a ubiquitous family of molecular chaperones that suppress the unspecific aggregation of miscellaneous proteins. Multicellular organisms contain a large number of different sHsps, raising questions as to whether they function redundantly or are specialized in terms of substrates and mechanism. To gain insight into this issue, we undertook a comparative analysis of the 8 major human sHsps on the aggregation of both model proteins and cytosolic lysates under standardized conditions...
November 30, 2016: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/27909014/sodium-4-phenylbutyrate-attenuates-myocardial-reperfusion-injury-by-reducing-the-unfolded-protein-response
#13
Osamu Takatori, Soichiro Usui, Masaki Okajima, Shuichi Kaneko, Hiroshi Ootsuji, Shin-Ichiro Takashima, Daisuke Kobayashi, Hisayoshi Murai, Hiroshi Furusho, Masayuki Takamura
BACKGROUND: The unfolded protein response (UPR) plays a pivotal role in ischemia-reperfusion (I/R) injury in various organs such as heart, brain, and liver. Sodium 4-phenylbutyrate (PBA) reportedly acts as a chemical chaperone that reduces UPR. In the present study, we evaluated the effect of PBA on reducing the UPR and protecting against myocardial I/R injury in mice. METHODS: Male C57BL/6 mice were subjected to 30-minute myocardial I/R, and were treated with phosphate-buffered saline (as a vehicle) or PBA...
December 1, 2016: Journal of Cardiovascular Pharmacology and Therapeutics
https://www.readbyqxmd.com/read/27908666/molecular-cloning-and-expression-analysis-of-five-heat-shock-protein-70-hsp70-family-members-in-lateolabrax-maculatus-with-vibrio-harveyi-infection
#14
Ying-Li Han, Cong-Cong Hou, Chen Du, Jun-Quan Zhu
Heat shock proteins 70 (HSP70s) are molecular chaperones that aid in protection against environmental stress. In this study, we cloned and characterized five members of the HSP70 family (designated as HSPa1a, HSC70-1, HSC70-2, HSPa4 and HSPa14) from Lateolabrax maculatus using rapid amplification cDNA ends (RACE). Multiple sequence alignment and structural analysis revealed that all members of the HSP70 family had a conserved domain architecture, with some distinguishing features unique to each HSP70. Quantitative real-time (qPCR) analysis revealed that all members of the HSP70 family were ubiquitously and differentially expressed in all major types of tissues, including testicular tissue...
November 28, 2016: Fish & Shellfish Immunology
https://www.readbyqxmd.com/read/27908229/localization-of-nuclear-encoded-mrnas-to-mitochondria-outer-surface
#15
REVIEW
A Golani-Armon, Y Arava
The diverse functions of mitochondria depend on hundreds of different proteins. The vast majority of these proteins is encoded in the nucleus, translated in the cytosol, and must be imported into the organelle. Import was shown to occur after complete synthesis of the protein, with the assistance of cytosolic chaperones that maintain it in an unfolded state and target it to the mitochondrial translocase of the outer membrane (TOM complex). Recent studies, however, identified many mRNAs encoding mitochondrial proteins near the outer membrane of mitochondria...
October 2016: Biochemistry. Biokhimii︠a︡
https://www.readbyqxmd.com/read/27907150/molecular-characterization-of-two-monoclonal-antibodies-against-the-same-epitope-on-b-cell-receptor-associated-protein-31
#16
Won-Tae Kim, Saemina Shin, Hyo Jeong Hwang, Min Kyu Kim, Han-Sung Jung, Hwangseo Park, Chun Jeih Ryu
Previously, we showed that B-cell receptor associated protein 31 (BAP31), an endoplasmic reticulum (ER) membrane chaperone, is also expressed on the cell surface by two monoclonal antibodies (MAbs) 297-D4 and 144-A8. Both MAbs recognize the same linear epitope on the C-terminal domain of BAP31, although they were independently established. Here, flow cytometric analysis showed that 144-A8 had additional binding properties to some cells, as compared to 297-D4. Quantitative antigen binding assays also showed that 144-A8 had higher antigen binding capacity than 297-D4...
2016: PloS One
https://www.readbyqxmd.com/read/27906968/structural-and-functional-recovery-of-sensory-cilia-in-c-elegans-ift-mutants-upon-aging
#17
Astrid Cornils, Ashish K Maurya, Lauren Tereshko, Julie Kennedy, Andrea G Brear, Veena Prahlad, Oliver E Blacque, Piali Sengupta
The majority of cilia are formed and maintained by the highly conserved process of intraflagellar transport (IFT). Mutations in IFT genes lead to ciliary structural defects and systemic disorders termed ciliopathies. Here we show that the severely truncated sensory cilia of hypomorphic IFT mutants in C. elegans transiently elongate during a discrete period of adult aging leading to markedly improved sensory behaviors. Age-dependent restoration of cilia morphology occurs in structurally diverse cilia types and requires IFT...
December 2016: PLoS Genetics
https://www.readbyqxmd.com/read/27906033/the-role-of-the-backbone-torsion-in-protein-folding
#18
EDITORIAL
Irina Sorokina, Arcady Mushegian
BACKGROUND: The set of forces and sequence of events that govern the transition from an unfolded polypeptide chain to a functional protein with correct spatial structure remain incompletely known, despite the importance of the problem and decades of theory development, computer simulations, and laboratory experiments. Information about the correctly folded state of most proteins is likely to be present in their sequences, and yet many proteins fail to attain native structure after overexpression in a non-native environment or upon experimental denaturation and refolding...
December 1, 2016: Biology Direct
https://www.readbyqxmd.com/read/27905509/the-er-stress-regulator-bip-mediates-cadmium-induced-autophagy-and-neuronal-senescence
#19
Tao Wang, Yan Yuan, Hui Zou, Jinlong Yang, Shiwen Zhao, Yonggang Ma, Yi Wang, Jianchun Bian, Xuezhong Liu, Jianhong Gu, Zongping Liu, Jiaqiao Zhu
Autophagy is protective in cadmium (Cd)-induced oxidative damage. Endoplasmic reticulum (ER) stress has been shown to induce autophagy in a process requiring the unfolded protein response signalling pathways. Cd treatment significantly increased senescence in neuronal cells, which was aggravated by 3-MA or silencing of Atg5 and abolished by rapamycin. Cd increased expression of ER stress regulators Bip, chop, eIf2α, and ATF4, and activated autophagy as evidenced by upregulated LC3. Moreover, the ER stress inhibitor mithramycin inhibited the expression of ER stress protein chaperone Bip and blocked autophagic flux...
December 1, 2016: Scientific Reports
https://www.readbyqxmd.com/read/27904835/a-novel-dominant-d109a-cryab-mutation-in-a-family-with-myofibrillar-myopathy-affects-%C3%AE-b-crystallin-structure
#20
Jakub P Fichna, Anna Potulska-Chromik, Przemysław Miszta, Maria Jolanta Redowicz, Anna M Kaminska, Cezary Zekanowski, Sławomir Filipek
Myofibrillar myopathy (MFM) is a group of inherited muscular disorders characterized by myofibrils dissolution and abnormal accumulation of degradation products. So far causative mutations have been identified in nine genes encoding Z-disk proteins, including αB-crystallin (CRYAB), a small heat shock protein (also called HSPB5). Here, we report a case study of a 63-year-old Polish female with a progressive lower limb weakness and muscle biopsy suggesting a myofibrillar myopathy, and extra-muscular multisystemic involvement, including cataract and cardiomiopathy...
June 2017: BBA Clinical
keyword
keyword
83924
1
2
Fetch more papers »
Fetching more papers... Fetching...
Read by QxMD. Sign in or create an account to discover new knowledge that matter to you.
Remove bar
Read by QxMD icon Read
×

Search Tips

Use Boolean operators: AND/OR

diabetic AND foot
diabetes OR diabetic

Exclude a word using the 'minus' sign

Virchow -triad

Use Parentheses

water AND (cup OR glass)

Add an asterisk (*) at end of a word to include word stems

Neuro* will search for Neurology, Neuroscientist, Neurological, and so on

Use quotes to search for an exact phrase

"primary prevention of cancer"
(heart or cardiac or cardio*) AND arrest -"American Heart Association"