Analysis of Arabidopsis thioredoxin-h isotypes identifies discrete domains that confer specific structural and functional properties

2013 ◽  
Vol 456 (1) ◽  
pp. 13-24 ◽  
Author(s):  
Young Jun Jung ◽  
Yong Hun Chi ◽  
Ho Byoung Chae ◽  
Mi Rim Shin ◽  
Eun Seon Lee ◽  
...  
Keyword(s):  
Amino Acids ◽  
Heat Shock ◽  
Functional Properties ◽  
Critical Role ◽  
Chaperone Function ◽  
Structural And Functional Properties ◽  
Shock Resistance ◽  
Thioredoxin H ◽  
Discrete Domains

In this study, we identified specific domains and amino acids responsible for the structural and functional properties of AtTrx-hs (Arabidopsis h-type thioredoxins). Specific domains and amino acids for the chaperone function of AtTrx-hs played a critical role in heat-shock-resistance in vivo.

scholarly journals Profibrillatory Structural and Functional Properties of the Atrial-Pulmonary Junction in the Absence of Remodeling

2021 ◽  
Vol 12 ◽  
Author(s):  
Lisa A. Gottlieb ◽  
Charly Belterman ◽  
Shirley van Amersfoorth ◽  
Virginie Loyer ◽  
Marion Constantin ◽  
...  
Keyword(s):  
Functional Properties ◽  
Histological Analysis ◽  
Atrial Arrhythmias ◽  
Fat Tissue ◽  
Stimulation Threshold ◽  
Ablation Therapy ◽  
Structural And Functional Properties ◽  
Healthy Sheep ◽  
Electrophysiological Studies

Background: Sole pulmonary vein (PV) isolation by ablation therapy prevents atrial fibrillation (AF) in patients with short episodes of AF and without comorbidities. Since incomplete PV isolation can be curative, we tested the hypothesis that the PV in the absence of remodeling and comorbidities contains structural and functional properties that are proarrhythmic for AF initiation by reentry.Methods: We performed percutaneous transvenous in vivo endocardial electrophysiological studies and quantitative histological analysis of PV from healthy sheep.Results: The proximal PV contained more myocytes than the distal PV and a higher percentage of collagen and fat tissue relative to myocytes than the left atrium. Local fractionated electrograms occurred in both the distal and proximal PVs, but a large local activation (>0.75 mV) was more often present in the proximal PV than in the distal PV (86 vs. 50% of electrograms, respectively, p = 0.017). Atrial arrhythmias (run of premature atrial complexes) occurred more often following the premature stimulation in the proximal PV than in the distal PV (p = 0.004). The diastolic stimulation threshold was higher in the proximal PV than in the distal PV (0.7 [0.3] vs. 0.4 [0.2] mA, (median [interquartile range]), p = 0.004). The refractory period was shorter in the proximal PV than in the distal PV (170 [50] vs. 248 [52] ms, p < 0.001). A linear relation existed between the gradient in refractoriness (distal-proximal) and atrial arrhythmia inducibility in the proximal PV.Conclusion: The structural and functional properties of the native atrial-PV junction differ from those of the distal PV. Atrial arrhythmias in the absence of arrhythmia-induced remodeling are caused by reentry in the atrial-PV junction. Ablative treatment of early paroxysmal AF, rather than complete isolation of focal arrhythmia, may be limited to inhibition of reentry.

scholarly journals Structural and functional properties of CiNTH, an endonuclease III homologue of the ascidian Ciona intestinalis: critical role of N-terminal region

2012 ◽  
Vol 87 (2) ◽  
pp. 115-124 ◽  
Author(s):  
Seiji Kato ◽  
Kazunari Hashiguchi ◽  
Kento Igarashi ◽  
Takahito Moriwaki ◽  
Shin-Ichiro Yonekura ◽  
...  
Keyword(s):  
Functional Properties ◽  
Critical Role ◽  
Ciona Intestinalis ◽  
Terminal Region ◽  
Endonuclease Iii ◽  
Structural And Functional Properties

scholarly journals Optimal Activation of an Endogenous Gene by HOX11 Requires the NH2-Terminal 50 Amino Acids

1998 ◽  
Vol 18 (6) ◽  
pp. 3502-3508 ◽  
Author(s):  
Norma Masson ◽  
Wayne K. Greene ◽  
Terence H. Rabbitts
Keyword(s):  
Amino Acids ◽  
Transcriptional Control ◽  
Target Genes ◽  
Critical Role ◽  
Homeobox Gene ◽  
Terminal Region ◽  
Endogenous Gene ◽  
Murine Spleen ◽  
Nih 3T3

ABSTRACT The HOX11 homeobox gene was first identified through studies of the t(7;10) and t(10;14) chromosomal translocations of acute T-cell leukemia. In addition, analysis of Hox11−/− mice has demonstrated a critical role for this gene in murine spleen development. A possible mode of in vivo function for the HOX11 protein in these two situations is regulation of target genes following DNA binding via the homeodomain, but little is known about how HOX11 regulates transcription in vivo. By performing transcriptional studies in yeast and mammalian one-hybrid systems, a modular transcriptional transactivation region at the NH2 terminus of HOX11 has been functionally dissected from other parts of the protein. This NH2-terminal region includes the previously identified short conserved Hep motif, which itself activates transcription in one-hybrid assays. The importance of the NH2-terminal region for the function of HOX11 in vivo was assayed by activating a HOX11-dependent gene in NIH 3T3 cells. Activation of this gene was found to be dependent upon an intact homeodomain in HOX11, but maximal activation was obtained only when the NH2-terminal 50 amino acids of HOX11 was present, showing that this region of HOX11 is important for in vivo transcriptional control of a chromosomal target gene.

scholarly journals Mitochondrial heat shock protein 70, a molecular chaperone for proteins encoded by mitochondrial DNA.

1994 ◽  
Vol 127 (4) ◽  
pp. 893-902 ◽  
Author(s):  
J M Herrmann ◽  
R A Stuart ◽  
E A Craig ◽  
W Neupert
Keyword(s):  
Mitochondrial Dna ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Critical Role ◽  
Molecular Complexes ◽  
Mitochondrial Ribosomes ◽  
Mitochondrial Heat Shock Protein

Mitochondrial heat shock protein 70 (mt-Hsp70) has been shown to play an important role in facilitating import into, as well as folding and assembly of nuclear-encoded proteins in the mitochondrial matrix. Here, we describe a role for mt-Hsp70 in chaperoning proteins encoded by mitochondrial DNA and synthesized within mitochondria. The availability of mt-Hsp70 function influences the pattern of proteins synthesized in mitochondria of yeast both in vivo and in vitro. In particular, we show that mt-Hsp70 acts in maintaining the var1 protein, the only mitochondrially encoded subunit of mitochondrial ribosomes, in an assembly competent state, especially under heat stress conditions. Furthermore, mt-Hsp70 helps to facilitate assembly of mitochondrially encoded subunits of the ATP synthase complex. By interacting with the ATP-ase 9 oligomer, mt-Hsp70 promotes assembly of ATP-ase 6, and thereby protects the latter protein from proteolytic degradation. Thus mt-Hsp70 by acting as a chaperone for proteins encoded by the mitochondrial DNA, has a critical role in the assembly of supra-molecular complexes.

scholarly journals Detailed characterization of the UMAMITs provides insight into their evolution, functional properties as amino acid transporters and role in the plant

2021 ◽  
Author(s):  
Chengsong Zhao ◽  
Réjane Pratelli ◽  
Shi Yu ◽  
Brett Shelley ◽  
Eva Collakova ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Functional Properties ◽  
Critical Role ◽  
Amino Acid Transporters ◽  
Cell Compartments ◽  
Transporter Family ◽  
Insight Into

AbstractAmino acid transporters play a critical role in distributing amino acids within the cell compartments and between the plant organs. Despite this importance, relatively few amino acid transporter genes have been characterized and their role elucidated with certainty. Two main families of proteins encode amino acid transporters in plants: the Amino Acid-Polyamine-Organocation superfamily, containing mostly importers, and the Usually Multiple Acids Move In and out Transporter family, apparently encoding exporters, totaling about 100 genes in Arabidopsis alone. Knowledge on UMAMITs is scarce, focused on six Arabidopsis genes and a handful of genes from other species. To get insight into the role of the members of this family and provide data to be used for future characterization, we studied the evolution of the UMAMITs in plants, and determined the functional properties, the structure, and the localization of the 44 Arabidopsis UMAMITs. Our analysis showed that the AtUMAMIT are essentially localized at the tonoplast or the plasma membrane, and that most of them are able to export amino acids from the cytosol, confirming a role in intra- and inter-cellular amino acid transport. As an example, this set of data was used to hypothesize the role of a few AtUMAMITs in the plant and the cell.

scholarly journals Bridging the Knowledge Gap for the Impact of Non-Thermal Processing on Proteins and Amino Acids

Foods ◽  
2019 ◽  
Vol 8 (7) ◽  
pp. 262 ◽  
Author(s):  
Sara Esteghlal ◽  
Hadi Hashemi Gahruie ◽  
Mehrdad Niakousari ◽  
Francisco J. Barba ◽  
Alaa El-Din Bekhit ◽  
...  
Keyword(s):  
Amino Acids ◽  
Functional Properties ◽  
Thermal Processing ◽  
Thermal Treatments ◽  
Processing Technologies ◽  
Structural And Functional Properties ◽  
Wide Range ◽  
Protein Properties ◽  
The Impact ◽  
Structure Of Proteins

Proteins represent one of the major food components that contribute to a wide range of biophysical functions and dictate the nutritional, sensorial, and shelf-life of food products. Different non-thermal processing technologies (e.g., irradiation, ultrasound, cold plasma, pulsed electric field, and high-pressure treatments) can affect the structure of proteins, and thus their solubility as well as their functional properties. The exposure of hydrophobic groups, unfolding followed by aggregation at high non-thermal treatment intensities, and the formation of new bonds have been reported to promote the modification of structural and functional properties of proteins. Several studies reported the reduction of allergenicity of some proteins after the application of non-thermal treatments. The composition and concentration of free amino acids could be changed after non-thermal processing, depending on the processing time and intensity. The present review discusses the effects of different non-thermal treatments on protein properties in detail, and highlights the opportunities and disadvantages of these technologies in relation to protein functionality.

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