Conformational and functional studies of a cytosolic 90 kDa heat shock protein Hsp90 from sugarcane

Silva, Viviane C. H. da; Cagliari, Thiago C.; Lima, Tatiani B.; Gozzo, Fábio C.; Ramos, Carlos H.I.

doi:10.1016/j.plaphy.2013.03.015

Cited by 17 publications

(13 citation statements)

References 46 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Chemical Cross-linking Coupled to Mass Spectrometry (XL-MS)-Cross-linking reactions were performed as described previously (30,31). Briefly, protein preparations in isolated or complex forms were incubated in 20 mM Hepes (pH 7.5) with DSS in a 1:50 ratio (complex:DSS) for 2 h at room temperature and the cross-linking reaction was quenched with 100 mM ammonium bicarbonate (pH 8.0).…”

Section: Methodsmentioning

confidence: 99%

Heat Shock Protein 90 kDa (Hsp90) Has a Second Functional Interaction Site with the Mitochondrial Import Receptor Tom70

Zanphorlin

Lima

Wong

et al. 2016

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

To accomplish its crucial role, mitochondria require proteins that are produced in the cytosol, delivered by cytosolic Hsp90, and translocated to its interior by the translocase outer membrane (TOM) complex. Hsp90 is a dimeric molecular chaperone and its function is modulated by its interaction with a large variety of co-chaperones expressed within the cell. An important family of co-chaperones is characterized by the presence of one TPR (tetratricopeptide repeat) domain, which binds to the C-terminal MEEVD motif of Hsp90. These include Tom70, an important component of the TOM complex. Despite a wealth of studies conducted on the relevance of Tom70·Hsp90 complex formation, there is a dearth of information regarding the exact molecular mode of interaction. To help fill this void, we have employed a combined experimental strategy consisting of cross-linking/mass spectrometry to investigate binding of the C-terminal Hsp90 domain to the cytosolic domain of Tom70. This approach has identified a novel region of contact between C-Hsp90 and Tom70, a finding that is confirmed by probing the corresponding peptides derived from cross-linking experiments via isothermal titration calorimetry and mitochondrial import assays. The data generated in this study are combined to input constraints for a molecular model of the Hsp90/Tom70 interaction, which has been validated by small angle x-ray scattering, hydrogen/deuterium exchange, and mass spectrometry. The resultant model suggests that only one of the MEEVD motifs within dimeric Hsp90 contacts Tom70. Collectively, our findings provide significant insight on the mechanisms by which preproteins interact with Hsp90 and are translocated via Tom70 to the mitochondria.

show abstract

Section: Methodsmentioning

confidence: 99%

Heat Shock Protein 90 kDa (Hsp90) Has a Second Functional Interaction Site with the Mitochondrial Import Receptor Tom70

Zanphorlin

Lima

Wong

et al. 2016

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

show abstract

“…Briefly, A. thaliana Columbia‐0 (Col‐0) was cultivated on a mixture of soil and vermiculite (1:1) or in Murashige and Skoog medium (1/2 MS). Plants were transformed through Agrobacterium ‐mediated transformation, as previously described . Agrobacterium tumefaciens (GV3101:pMP90 strain carrying the binary vector pCAMBIA 2300, containing nptII gene under control of CaMV 35S was sprayed over the plants just before bolting.…”

Section: Methodsmentioning

confidence: 99%

Comparative proteomics and metallomics studies in Arabidopsis thaliana leaf tissues: Evaluation of the selenium addition in transgenic and nontransgenic plants using two‐dimensional difference gel electrophoresis and laser ablation imaging

et al. 2014

View full text Add to dashboard Cite

The main goal of this work is to evaluate some differential protein species in transgenic (T) and nontransgenic (NT) Arabidopsis thaliana plants after their cultivation in the presence or absence of sodium selenite. The transgenic line was obtained through insertion of CaMV 35S controlling nptII gene. Comparative proteomics through 2D-DIGE is carried out in four different groups (NT × T; NT × Se-NT (where Se is selenium); Se-NT × Se-T, and T × Se-T). Although no differential proteins are achieved in the T × Se-T group, for the others, 68 differential proteins (by applying a regulation factor ≥1.5) are achieved, and 27 of them accurately characterized by ESI-MS/MS. These proteins are classified into metabolism, energy, signal transduction, disease/defense categories, and some of them are involved in the glycolysis pathway-Photosystems I and II and ROS combat. Additionally, laser ablation imaging is used for evaluating the Se and sulfur distribution in leaves of different groups, corroborating some results obtained and related to proteins involved in the glycolysis pathway. From these results, it is possible to conclude that the genetic modification also confers to the plant resistance to oxidative stress.

show abstract

“…Solution NMR methodology was used to elucidate the structure and dynamics of Sd5, a defensin from Saccharum officinarum . Structural conformation of HSP 90 from sugarcane was elucidated by hydrogen/deuterium exchange using MS, hydrodynamic assays, and CD . Tiroli et al.…”

Section: Structural Proteomicsmentioning

confidence: 99%

“…Solution NMR methodology was used to elucidate the structure and dynamics of Sd5, a defensin from Saccharum officinarum [75]. Structural conformation of HSP 90 from sugarcane was elucidated by hydrogen/deuterium exchange using MS, hydrodynamic assays, and CD [76]. Tiroli et al [77] has characterized and elucidated the structural conformation of chaperone Hsp70 from sugarcane by chemical cross-linking coupled to MS. A heme-binding globin in sugarcane was also structurally characterized by CD [78].…”

Section: Structural Proteomicsmentioning

confidence: 99%

Sugarcane proteomics: An update on current status, challenges, and future prospects

et al. 2015

View full text Add to dashboard Cite

Sugarcane is one of the most important commercial crops cultivated worldwide for the production of crystal sugar, ethanol, and other related by-products. Unlike other comparable monocots like sorghum, maize, and rice, sugarcane genome by virtue of its polyploidy nature remains yet to be fully deciphered. Proteomics-an established complementary tool to genomics is at its infancy in sugarcane as compared to the other monocots. However, with the surge in genomics research accomplished by next-generation sequencing platforms, sugarcane proteomics has gained momentum. This review summarizes the available literature from 1970 to 2014, which ensures a comprehensive coverage on sugarcane proteomics-a topic first of its kind to be reviewed. We herewith compiled substantial contributions in different areas of sugarcane proteomics, which include abiotic and biotic stresses, cell wall, organelle, and structural proteomics. The past decade has witnessed a paradigm shift in the pace with which sugarcane proteomics is progressing, as evident by the number of research publications. In addition to extensively reviewing the progress made thus far, we intend to highlight the scope in sugarcane proteomics, with an aspiration to instigate focused research on sugarcane to harness its full potential for the human welfare.

show abstract

Conformational and functional studies of a cytosolic 90 kDa heat shock protein Hsp90 from sugarcane

Cited by 17 publications

References 46 publications

Heat Shock Protein 90 kDa (Hsp90) Has a Second Functional Interaction Site with the Mitochondrial Import Receptor Tom70

Heat Shock Protein 90 kDa (Hsp90) Has a Second Functional Interaction Site with the Mitochondrial Import Receptor Tom70

Comparative proteomics and metallomics studies in Arabidopsis thaliana leaf tissues: Evaluation of the selenium addition in transgenic and nontransgenic plants using two‐dimensional difference gel electrophoresis and laser ablation imaging

Sugarcane proteomics: An update on current status, challenges, and future prospects

Contact Info

Product

Resources

About