scholarly journals Structure and function of an Arabidopsis thaliana sulfate transporter

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Lie Wang ◽  
Kehan Chen ◽  
Ming Zhou

AbstractPlant sulfate transporters (SULTR) mediate absorption and distribution of sulfate (SO42−) and are essential for plant growth; however, our understanding of their structures and functions remains inadequate. Here we present the structure of a SULTR from Arabidopsis thaliana, AtSULTR4;1, in complex with SO42− at an overall resolution of 2.8 Å. AtSULTR4;1 forms a homodimer and has a structural fold typical of the SLC26 family of anion transporters. The bound SO42− is coordinated by side-chain hydroxyls and backbone amides, and further stabilized electrostatically by the conserved Arg393 and two helix dipoles. Proton and SO42− are co-transported by AtSULTR4;1 and a proton gradient significantly enhances SO42− transport. Glu347, which is ~7 Å from the bound SO42−, is required for H+-driven transport. The cytosolic STAS domain interacts with transmembrane domains, and deletion of the STAS domain or mutations to the interface compromises dimer formation and reduces SO42− transport, suggesting a regulatory function of the STAS domain.

2020 ◽  
Vol 6 (1) ◽  
pp. 34
Author(s):  
Shangkun Qiu ◽  
Bin Zeng

Acyl-CoA-binding protein (ACBP) is an important protein with a size of about 10 kDa. It has a high binding affinity for C12–C22 acyl-CoA esters and participates in lipid metabolism. ACBP and its family of proteins have been found in all eukaryotes and some prokaryotes. Studies have described the function and structure of ACBP family proteins in mammals (such as humans and mice), plants (such as Oryza sativa, Arabidopsis thaliana, and Hevea brasiliensis) and yeast. However, little information on the structure and function of the proteins in filamentous fungi has been reported. This article concentrates on recent advances in the research of the ACBP family proteins in plants and mammals, especially in yeast, filamentous fungi (such as Monascus ruber and Aspergillus oryzae), and fungal pathogens (Aspergillus flavus, Cryptococcus neoformans). Furthermore, we discuss some problems in the field, summarize the binding characteristics of the ACBP family proteins in filamentous fungi and yeast, and consider the future of ACBP development.


Plants ◽  
2020 ◽  
Vol 9 (11) ◽  
pp. 1435
Author(s):  
Janardan Khadka ◽  
Anat Pesok ◽  
Gideon Grafi

Besides chemical modification of histone proteins, chromatin dynamics can be modulated by histone variants. Most organisms possess multiple genes encoding for core histone proteins, which are highly similar in amino acid sequence. The Arabidopsis thaliana genome contains 11 genes encoding for histone H2B (HTBs), 13 for H2A (HTAs), 15 for H3 (HTRs), and 8 genes encoding for histone H4 (HFOs). The finding that histone variants may be expressed in specific tissues and/or during specific developmental stages, often displaying specific nuclear localization and involvement in specific nuclear processes suggests that histone variants have evolved to carry out specific functions in regulating chromatin structure and function and might be important for better understanding of growth and development and particularly the response to stress. In this review, we will elaborate on a group of core histone proteins in Arabidopsis, namely histone H2B, summarize existing data, and illuminate the potential function of H2B variants in regulating chromatin structure and function in Arabidopsis thaliana.


Antioxidants ◽  
2019 ◽  
Vol 8 (1) ◽  
pp. 8 ◽  
Author(s):  
Aleksandra Lewandowska ◽  
Trung Nghia Vo ◽  
Thuy-Dung Ho Nguyen ◽  
Khadija Wahni ◽  
Didier Vertommen ◽  
...  

Members of the DJ-1 protein family are multifunctional enzymes whose loss increases the susceptibility of the cell to oxidative stress. However, little is known about the function of the plant DJ-1 homologs. Therefore, we analyzed the effect of oxidation on the structure and function of chloroplastic AtDJ-1B and studied the phenotype of T-DNA lines lacking the protein. In vitro oxidation of AtDJ-1B with H2O2 lowers its glyoxalase activity, but has no effect on its holdase chaperone function. Remarkably, upon oxidation, the thermostability of AtDJ-1B increases with no significant alteration of the overall secondary structure. Moreover, we found that AtDJ-1B transcript levels are invariable, and loss of AtDJ-1B does not affect plant viability, growth and stress response. All in all, two discrete functions of AtDJ-1B respond differently to H2O2, and AtDJ-1B is not essential for plant development under stress.


1998 ◽  
Vol 76 (2-3) ◽  
pp. 359-367 ◽  
Author(s):  
E Bruce Waygood

Histidine-containing phosphocarrier protein, HPr, was one of the early protein tertiary structures determined by two-dimensional 1H-NMR. Tertiary structures for HPrs from Escherichia coli, Bacillus subtilis, and Staphylococcus aureus have been obtained by 1H NMR and the overall folding pattern of HPr is highly conserved, a beta alpha beta beta alpha beta alpha arrangement of three alpha-helices overlaying a four-stranded beta-sheet. High-resolution structures for HPrs from E. coli and B. subtilis have been obtained using 15N- and 13C-labeled proteins. The first application of NMR to the understanding of the structure and function of HPr was to describe the phosphohistidine isomer, Ndelta1-P-histidine in S. aureus phospho-HPr, and the unusual pKas of the His-15 side chain. The pKa values for the His-15 imidazole from more recent studies are 5.4 for HPr and 7.8 for phospho-HPr from E. coli, for example. A consensus description of the active site is proposed for HPr and phospho-HPr. In HPr, His-15 has a defined conformation and N-caps helix A, and is thus affected by the helix dipole. His-15 undergoes a small conformational change upon phosphorylation, a movement to allow the phosphoryl group to be positioned such that it forms hydrogen bonds with the main chain amide nitrogens of residue 16 (not conserved) and Arg-17. Interactions between residue 12 side chain (not conserved: asparagine, serine, and threonine) and His-15, and between the Arg-17 guanidinium group and the phosphoryl group, are either weak or transitory.Key words: HPr, NMR, phosphoenolpyruvate:sugar phosphotransferase system, phosphohistidine, phosphoserine.


2021 ◽  
Vol 18 (1) ◽  
Author(s):  
Grets Lewis Theodore Walilo

Penelitian ini bertujuan untuk memahami struktur dan fungsi dari bahasa Hubula di lembah Balim Papua dengan perkembangannya dalam era modern. Bahasa ini memiliki pola kalimat yang mudah untuk diidentifikasi. Penelitian ini dilakukan dengan pendekatan sosiolinguistik yang berfokus pada pemakaian bahasa dalam masyarakat untuk menjalankan fungsi-fungsi yang terkandung. Hasilnya ditemukan bahwa bahasa Hubula masih diminati di Lembah Balim bahkan dalam era modern. Dengan menguasai beberapa kata-kata dasar, struktur dari pada kalimat Bahasa Hubula dapat diidentifikasi dengan mudah. Sebagai jembatan untuk berinteraksi, bahasa ini memiliki beberapa fungsi seperti fungsi personal, fungsi informatif, fungsi interaksional, dan fungsi regulatoris. Kata kunci: bahasa Hubula, struktur bahasa, fungsi bahasa, era modern   The purpose of this study is to understand the structure and function of Hubula tribe language from Balim Valley Papua with its development in the modern era. Whereas, the language has an easy sentence pattern to be identified. This research was conducted with a sociolinguistic approach that focused on the usage of language in the society to perform its function. The result showed that Hubula tribe language is still favorable in Balim Valley even at the modern era. By knowing some basic vocabularies, the sentence’s structure of Hubula tribe language can be identified easily. As the bridge for interaction, this language has several functions such as; personal function, informative function, interaction function and regulatory function. Key words: Hubula tribe language, language’s structure, language’s function, modern era    


2011 ◽  
Vol 28 (3) ◽  
pp. 407-422 ◽  
Author(s):  
Alok K. Sharma ◽  
Alan C. Rigby ◽  
Seth L. Alper

2006 ◽  
Vol 38 (2) ◽  
pp. 327-341 ◽  
Author(s):  
Alfredo Pérez-de-Mora ◽  
Pilar Burgos ◽  
Engracia Madejón ◽  
Francisco Cabrera ◽  
Petra Jaeckel ◽  
...  

2007 ◽  
Vol 35 (5) ◽  
pp. 870-875 ◽  
Author(s):  
C.J. Schofield ◽  
M.A. McDonough

Phytanic acid (PA) is an epimeric metabolite of the isoprenoid side chain of chlorophyll. Owing to the presence of its epimeric β-methyl group, PA cannot be metabolized by β-oxidation. Instead, it is metabolized in peroxisomes via α-oxidation to give pristanic acid, which is then oxidized by β-oxidation. PhyH (phytanoyl-CoA 2-hydroxylase, also known as PAHX), an Fe(II) and 2OG (2-oxoglutarate) oxygenase, catalyses hydroxylation of phytanoyl-CoA. Mutations of PhyH ablate its role in α-oxidation, resulting in PA accumulation and ARD (adult Refsum's disease). The structure and function of PhyH is discussed in terms of its clinical importance and unusual selectivity. Most point mutations of PhyH causing ARD cluster in two distinct groups around the Fe(II)- and 2OG-binding sites. Therapaeutic possibilities for the treatment of Refsum's disease involving PhyH are discussed.


Sign in / Sign up

Export Citation Format

Share Document