Evolutionary Analysis of the Steroidogenic Acute Regulatory Protein-Related Lipid Transfer Domain and Its Response to Salt Stress In Vitis Vinifera

2021 ◽  
Author(s):  
Honghong He ◽  
Huiming Gou ◽  
Qi Zhou ◽  
Xuejing Cao ◽  
Ping Wang ◽  
...  
Keyword(s):  
Salt Stress ◽  
Vitis Vinifera ◽  
Gene Family ◽  
Tertiary Structure ◽  
Expression Profiles ◽  
Regulatory Protein ◽  
Steroidogenic Acute Regulatory Protein ◽  
Evolutionary Analysis ◽  
Lipid Transfer ◽  
Steroidogenic Acute Regulatory

Abstract This study aimed to enhance the understanding of the steroidogenic acute regulatory protein-related lipid transfer (START) domain in Vitis vinifera. A total of 23 members of the VvSTARD gene family were found, which could be divided into five groups. The analyses of the gene codon preference, selective pressure, and tandem replication events of the VvSTARD, AtSTARD, and OsSTARD genomes indicated that tandem replication events occured in grapes, Arabidopsis, and rice genomes. Eight lipid transporter proteins were found in the tertiary structure of the STARD gene family in grapes. The analysis of the expression profiles of the three species microarrays showed that the expression sites of the STARD gene and the response to abiotic stress in the same subgroup had similar characteristics. In addition, quantitative real-time polymerase chain reaction (qRT-PCR) was used to analyze the expression of the STARD gene family in grape leaves in response to different hormones and abiotic stresses, and the obtained results were the same as those predicted by the cis-elements and the expression profiles. Furthermore, 35S:STARD5:EGFP was successfully constructed to verify the subcellular prediction results, and the results showed that STARD5 was located in the nucleus. Through the identification of salt tolerance of transgenic tomato, STARD5 was found to regulate the salt stress of plants. Collectively, these data indicated that the VvSTARD gene family plays an important role in response to salt stress.

Cholesterol binding is a prerequisite for the activity of the steroidogenic acute regulatory protein (StAR)

2008 ◽  
Vol 412 (3) ◽  
pp. 553-562 ◽  
Author(s):  
Alireza Roostaee ◽  
Élie Barbar ◽  
Jean-Guy LeHoux ◽  
Pierre Lavigne
Keyword(s):  
Thermodynamic Stability ◽  
Tertiary Structure ◽  
Regulatory Protein ◽  
Biologically Active ◽  
Steroidogenic Acute Regulatory Protein ◽  
Proper Function ◽  
Stable Complex ◽  
Steroidogenic Acute Regulatory ◽  
Α Helix ◽  
Cholesterol Binding

Steroidogenesis depends on the delivery of cholesterol from the outer to the inner mitochondrial membrane by StAR (steroidogenic acute regulatory protein). However, the mechanism by which StAR binds to cholesterol and its importance in cholesterol transport are under debate. According to our proposed molecular model, StAR possesses a hydrophobic cavity, which can accommodate one cholesterol molecule. In the bound form, cholesterol interacts with hydrophobic side-chains located in the C-terminal α-helix 4, thereby favouring the folding of this helix. To verify this model experimentally, we have characterized the in vitro activity, overall structure, thermodynamic stability and cholesterol-binding affinity of StAR lacking the N-terminal 62 amino acid residues (termed N-62 StAR). This mature form is biologically active and has a well-defined tertiary structure. Addition of cholesterol to N-62 StAR led to an increase in the α-helical content and T° (melting temperature), indicating the formation of a stable complex. However, the mutation F267Q, which is located in the C-terminal helix interface lining the cholesterol-binding site, reduced the biological activity of StAR. Furthermore, the cholesterol-induced thermodynamic stability and the binding capacity of StAR were significantly diminished in the F267Q mutant. Titration of StAR with cholesterol yielded a 1:1 complex with an apparent KD of 3×10−8. These results support our model and indicate that StAR can readily bind to cholesterol with an apparent affinity that commensurates with monomeric cholesterol solubility in water. The proper function of the C-terminal α-helix is essential for the binding process.

scholarly journals StarD7 Gene Expression in Trophoblast Cells: Contribution of SF-1 and Wnt-β-Catenin Signaling

2011 ◽  
Vol 25 (8) ◽  
pp. 1364-1375 ◽  
Author(s):  
Viviana Rena ◽  
Jésica Flores-Martín ◽  
Sofía Angeletti ◽  
Graciela M. Panzetta-Dutari ◽  
Susana Genti-Raimondi
Keyword(s):  
Gene Expression ◽  
Intracellular Transport ◽  
Regulatory Protein ◽  
Steroidogenic Acute Regulatory Protein ◽  
Regulatory Sequences ◽  
Physical Interaction ◽  
Lipid Transfer ◽  
Amino Acid Mutations ◽  
Steroidogenic Acute Regulatory

Steroidogenic acute regulatory protein-related lipid transfer domain containing 7 (StarD7) is a poorly characterized member of the steroidogenic acute regulatory protein-related lipid transfer proteins, up-regulated in JEG-3 cells, involved in intracellular transport and metabolism of lipids. Previous studies dealing with the mechanisms underlying the human StarD7 gene expression led us to define the cis-acting regulatory sequences in the StarD7 promoter using as a model JEG-3 cells. These include a functional T cell-specific transcription factor 4 (TCF4) site involved in Wnt-β-catenin signaling. To understand these mechanisms in more depth, we examined the steroidogenic factor 1 (SF-1) contribution to StarD7 expression. Cotransfection experiments in JEG-3 cells point out that the StarD7 promoter is activated by SF-1, and this effect is increased by forskolin. EMSA using JEG-3 nuclear proteins demonstrated that SF-1 binds to the StarD7 promoter. Additionally, chromatin immunoprecipitation analysis indicated that SF-1 and β-catenin are bound in vivo to the StarD7 promoter. Reporter gene assays in combination with mutations in the SF-1 and TCF4 binding sites revealed that the StarD7 promoter is synergistically activated by SF-1 and β-catenin and that the TCF4 binding site (−614/−608) plays an important role in this activation. SF-1 amino acid mutations involved in the physical interaction with β-catenin abolished this activation; thus demonstrating that the contact between the two proteins is necessary for an efficient StarD7 transcriptional induction. Finally, these data suggest that β-catenin could function as a bridge between SF-1 and TCF4 forming a ternary complex, which would stimulate StarD7 expression. The SF-1 and β-catenin pathway convergence on StarD7 expression may have important implications in the phospholipid uptake and transport, contributing to the normal trophoblast development.

MLN64 and MENTHO, two mediators of endosomal cholesterol transport

2006 ◽  
Vol 34 (3) ◽  
pp. 343-345 ◽  
Author(s):  
F. Alpy ◽  
C. Tomasetto
Keyword(s):  
Metastatic Lymph Node ◽  
Regulatory Protein ◽  
Steroidogenic Acute Regulatory Protein ◽  
Cholesterol Transport ◽  
Lipid Transfer ◽  
Transmembrane Helices ◽  
Late Endosomes ◽  
Start Domain ◽  
Steroidogenic Acute Regulatory

MLN64 (metastatic lymph node 64) and MENTHO (MLN64 N-terminal homologue) are two late-endosomal proteins that share a conserved region of four transmembrane helices with three short intervening loops called the MENTAL domain (MLN64 N-terminal domain). This domain mediates MLN64 and MENTHO homo- and hetero-interactions, targets both proteins to late endosomes and binds cholesterol in vivo. In addition to the MENTAL domain, MLN64 contains a cholesterol-specific START domain [StAR (steroidogenic acute regulatory protein)-related lipid transfer domain]. The START domain is a protein module of approx. 210 residues that binds lipids, including sterols, and is present in 15 distinct proteins in mammals. Thus MLN64 and MENTHO define discrete cholesterol-containing subdomains within the membrane of late endosomes where they may function in cholesterol transport. The MENTAL domain might serve to maintain cholesterol at the membrane of late endosomes prior to its shuttle to cytoplasmic acceptor(s) through the START domain.

scholarly journals Identification and Evolutionary Characteristic Analysis of STARD Gene Family, and Overexpression VvSTARD5 Responses to Salt Stress in Tomato

2022 ◽  
Author(s):  
Honghong He ◽  
Shixiong lu ◽  
Huiming Gou ◽  
Xuejing Cao ◽  
Ping Wang ◽  
...  
Keyword(s):  
Salt Stress ◽  
Salt Tolerance ◽  
Gene Family ◽  
Tertiary Structure ◽  
Function Analysis ◽  
Expression Profiles ◽  
Regulatory Gene ◽  
Characteristic Analysis ◽  
Expression Levels ◽  
Qrt Pcr

Abstract This study aimed to have a full understanding of the steroidogenic acute regulatory gene family member and evolutionary relationship in grape. 23 VvSTARD gene members were identified and divided into five groups in different species. Analyses of the gene codon preference, selective pressure, and tandem duplication of the VvSTARD, AtSTARD, and OsSTARD genes indicated that synteny relationship occurred in grapes, Arabidopsis thaliana, and rice genomes. The 8 lipid transporter proteins were found in the tertiary structure of the STARD gene family in grape. Expression profiles of the three species microarrays showed that the expression levels of the STARD genes in different organs and the response to abiotic stress in the same subgroup had similar characteristics. In addition, analysis of the VvSTARD genes expression levels was detected in response to different hormones and abiotic stresses by quantitative real-time polymerase chain reaction (qRT-PCR), and the results were the same as those predicted by the cis-elements and the expression profiles. Meanwhile, VvSTARD5 gene was screened in high concentration NaCl treatment by qRT-PCR. Furthermore, the VvSTARD5 was located at the nucleus by subcellular location. Through the function analysis of salt tolerance in transgenic tomato, overexpression VvSTARD5 obviously improved tolerance to salt stress. Taken together, our findings Preliminary identify the functions of VvSTARD gene family and vertify STARD5 that be likely involved in regulating salt tolerance, which may have potential application molecular breeding in grape.

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