ArticleThe Journal of biological chemistry2008
An unusual intrinsically disordered protein from the model legume Lotus japonicus stabilizes proteins in vitro.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Diversity of hydrodynamic radii of intrinsically disordered proteins.European biophysics journal : EBJ · 2023Article
- Investigating Intrinsically Disordered Proteins With Brownian Dynamics.Frontiers in molecular biosciences · 2022Article
- Beta turn propensity and a model polymer scaling exponent identify intrinsically disordered phase-separating proteins.The Journal of biological chemistry · 2021Article
- Pleiotropic roles of late embryogenesis abundant proteins ofComputational and structural biotechnology journal · 2021Review
- Functional assessment of hydrophilic domains of late embryogenesis abundant proteins from distant organisms.Microbial biotechnology · 2019Article
- Characterization of Dehydrin protein, CdDHN4-L and CdDHN4-S, and their differential protective roles against abiotic stress in vitro.BMC plant biology · 2018Article
- Steric interference from intrinsically disordered regions controls dynamin-related protein 1 self-assembly during mitochondrial fission.Scientific reports · 2018Article
- DrwH, a novel WHy domain-containing hydrophobic LEA5C protein from Deinococcus radiodurans, protects enzymatic activity under oxidative stress.Scientific reports · 2017Article
- Intrinsic α helix propensities compact hydrodynamic radii in intrinsically disordered proteins.Proteins · 2017Article
- The Unstructured N-terminal Region of Arabidopsis Group 4 Late Embryogenesis Abundant (LEA) Proteins Is Required for Folding and for Chaperone-like Activity under Water Deficit.The Journal of biological chemistry · 2016Article
- Hydrodynamic Radii of Intrinsically Disordered Proteins Determined from Experimental Polyproline II Propensities.PLoS computational biology · 2016Article
- Parametrization of Backbone Flexibility in a Coarse-Grained Force Field for Proteins (COFFDROP) Derived from All-Atom Explicit-Solvent Molecular Dynamics Simulations of All Possible Two-Residue Peptides.Journal of chemical theory and computation · 2015Article
- Alanine and proline content modulate global sensitivity to discrete perturbations in disordered proteins.Proteins · 2014Article
- Multifarious roles of intrinsic disorder in proteins illustrate its broad impact on plant biology.The Plant cell · 2013Review
- Conditional disorder in chaperone action.Trends in biochemical sciences · 2012Review
- The lysine-rich motif of intrinsically disordered stress protein CDeT11-24 from Craterostigma plantagineum is responsible for phosphatidic acid binding and protection of enzymes from damaging effects caused by desiccation.Journal of experimental botany · 2012Article
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- Intrinsically disordered proteins as molecular shields.Molecular bioSystems · 2012Article
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- Intrinsically disordered proteins and their environment: effects of strong denaturants, temperature, pH, counter ions, membranes, binding partners, osmolytes, and macromolecular crowding.The protein journal · 2009Review
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7 authors.
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Abstract
Intrinsic structural disorder is a prevalent feature of proteins with chaperone activity. Using a complementary set of techniques, we have structurally characterized LjIDP1 (intrinsically disordered protein 1) from the model legume Lotus japonicus, and our results provide the first structural characterization of a member of the Lea5 protein family (PF03242). Contrary to in silico predictions, we show that LjIDP1 is intrinsically disordered and probably exists as an ensemble of conformations with limited residual beta-sheet, turn/loop, and polyproline II secondary structure. Furthermore, we show that LjIDP1 has an inherent propensity to undergo a large conformational shift, adopting a largely alpha-helical structure when it is dehydrated and in the presence of different detergents and alcohols. This is consistent with an overrepresentation of order-promoting residues in LjIDP1 compared with the average of intrinsically disordered proteins. In line with functioning as a chaperone, we show that LjIDP1 effectively prevents inactivation of two model enzymes under conditions that promote protein misfolding and aggregation. The LjIdp1 gene is expressed in all L. japonicus tissues tested. A higher expression level was found in the root tip proximal zone, in roots inoculated with compatible endosymbiotic M. loti, and in functional nitrogen-fixing root nodules. We suggest that the ability of LjIDP1 to prevent protein misfolding and aggregation may play a significant role in tissues, such as symbiotic root nodules, which are characterized by high metabolic activity.
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