scholarly journals Advances in Understanding the Acyl-CoA-Binding Protein in Plants, Mammals, Yeast, and Filamentous Fungi

2020 ◽  
Vol 6 (1) ◽  
pp. 34
Author(s):  
Shangkun Qiu ◽  
Bin Zeng
Keyword(s):  
Arabidopsis Thaliana ◽  
Oryza Sativa ◽  
Filamentous Fungi ◽  
Fungal Pathogens ◽  
Binding Protein ◽  
Structure And Function ◽  
Monascus Ruber ◽  
Binding Characteristics ◽  
And Function ◽  
High Binding Affinity

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.

Molecular and Functional Characterization of One Odorant-Binding Protein Gene OBP3 in Bemisia tabaci (Hemiptera: Aleyrodidae)

2019 ◽  
Author(s):  
Ran Wang ◽  
Yuan Hu ◽  
Peiling Wei ◽  
Cheng Qu ◽  
Chen Luo
Keyword(s):  
Host Plant ◽  
Bemisia Tabaci ◽  
Binding Protein ◽  
Insect Pest ◽  
Critical Role ◽  
Functional Characterization ◽  
Odorant Binding Protein ◽  
Binding Characteristics ◽  
And Function ◽  
Odorant Binding

Abstract Odorant binding proteins (OBPs) of insects play a critical role in chemical perceptions and choice of insect host plant. Bemisia tabaci is a notorious insect pest which can damage more than 600 plant species. In order to explore functions of OBPs in B. tabaci, here we investigated binding characteristics and function of odorant-binding protein 3 in B. tabaci (BtabOBP3). The results indicated that BtabOBP3 shows highly similar sequence with OBPs of other insects, including the typical signature motif of six cysteines. The recombinant BtabOBP3 protein was obtained, and the evaluation of binding affinities to tested volatiles of host plant was conducted, then the results indicated that β-ionone had significantly higher binding to BtabOBP3 among other tested plant volatiles. Furthermore, silencing of BtabOBP3 significantly altered choice behavior of B. tabaci to β-ionone. In conclusion, it has been demonstrated that BtabOBP3 exerts function as one carrier of β-ionone and the results could be contributed to reveal the mechanisms of choosing host plant in B. tabaci.

scholarly journals Structure and function of renin binding protein

1994 ◽  
Vol 46 (6) ◽  
pp. 1525-1527 ◽  
Author(s):  
Saori Takahashi ◽  
Hiroyasu Inoue ◽  
Kiyoshi Fukui ◽  
Yoshihiro Miyake
Keyword(s):  
Binding Protein ◽  
Structure And Function ◽  
And Function

scholarly journals Regulation of synaptic structure and function by palmitoylated AMPA receptor binding protein

2010 ◽  
Vol 43 (4) ◽  
pp. 341-352 ◽  
Author(s):  
Charu Misra ◽  
Sophie Restituito ◽  
Jainne Ferreira ◽  
Gerald A. Rameau ◽  
Jie Fu ◽  
...  
Keyword(s):  
Ampa Receptor ◽  
Receptor Binding ◽  
Binding Protein ◽  
Structure And Function ◽  
Synaptic Structure ◽  
Ampa Receptor Binding Protein ◽  
And Function ◽  
Receptor Binding Protein

scholarly journals Plant Histone HTB (H2B) Variants in Regulating Chromatin Structure and Function

Plants ◽  
2020 ◽  
Vol 9 (11) ◽  
pp. 1435
Author(s):  
Janardan Khadka ◽  
Anat Pesok ◽  
Gideon Grafi
Keyword(s):  
Arabidopsis Thaliana ◽  
Chromatin Structure ◽  
Developmental Stages ◽  
Histone Variants ◽  
Structure And Function ◽  
Core Histone ◽  
Histone H2b ◽  
Histone Proteins ◽  
Genes Encoding ◽  
And Function

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.

scholarly journals Structure and function of the C-terminal PABC domain of human poly(A)-binding protein

2001 ◽  
Vol 98 (8) ◽  
pp. 4409-4413 ◽  
Author(s):  
G. Kozlov ◽  
J.-F. Trempe ◽  
K. Khaleghpour ◽  
A. Kahvejian ◽  
I. Ekiel ◽  
...  
Keyword(s):  
Binding Protein ◽  
Structure And Function ◽  
And Function

scholarly journals Chromatin-Mediated Regulation of Genome Plasticity in Human Fungal Pathogens

Genes ◽  
2019 ◽  
Vol 10 (11) ◽  
pp. 855 ◽  
Author(s):  
Buscaino
Keyword(s):  
Candida Albicans ◽  
Aspergillus Fumigatus ◽  
Cryptococcus Neoformans ◽  
Fungal Pathogens ◽  
Environmental Changes ◽  
Structure And Function ◽  
Model Systems ◽  
Genome Plasticity ◽  
And Function ◽  
Heterochromatin Structure

Human fungal pathogens, such as Candida albicans, Aspergillus fumigatus and Cryptococcus neoformans, are a public health problem, causing millions of infections and killing almost half a million people annually. The ability of these pathogens to colonise almost every organ in the human body and cause life-threating infections relies on their capacity to adapt and thrive in diverse hostile host-niche environments. Stress-induced genome instability is a key adaptive strategy used by human fungal pathogens as it increases genetic diversity, thereby allowing selection of genotype(s) better adapted to a new environment. Heterochromatin represses gene expression and deleterious recombination and could play a key role in modulating genome stability in response to environmental changes. However, very little is known about heterochromatin structure and function in human fungal pathogens. In this review, I use our knowledge of heterochromatin structure and function in fungal model systems as a road map to review the role of heterochromatin in regulating genome plasticity in the most common human fungal pathogens: Candida albicans, Aspergillus fumigatus and Cryptococcus neoformans.

scholarly journals Structure and function of a novel calcium-binding protein, CaBPc, from cardiac muscle.

1991 ◽  
Vol 55 ◽  
pp. 96
Author(s):  
Michiko Naka ◽  
Toshiya Sasaki ◽  
Hideaki Kise ◽  
Isao Tawara ◽  
Satoshi Hamaguchi ◽  
...  
Keyword(s):  
Cardiac Muscle ◽  
Calcium Binding ◽  
Binding Protein ◽  
Structure And Function ◽  
Calcium Binding Protein ◽  
And Function

scholarly journals Bifunctional Chloroplastic DJ-1B from Arabidopsis thaliana is an Oxidation-Robust Holdase and a Glyoxalase Sensitive to H2O2

Antioxidants ◽  
2019 ◽  
Vol 8 (1) ◽  
pp. 8 ◽  
Author(s):  
Aleksandra Lewandowska ◽  
Trung Nghia Vo ◽  
Thuy-Dung Ho Nguyen ◽  
Khadija Wahni ◽  
Didier Vertommen ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Arabidopsis Thaliana ◽  
Secondary Structure ◽  
Structure And Function ◽  
Transcript Levels ◽  
Chaperone Function ◽  
Multifunctional Enzymes ◽  
And Function ◽  
Discrete Functions

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.

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