Kinetic regulation mechanism of pbuE riboswitch

2015 ◽  
Vol 142 (1) ◽  
pp. 015103 ◽  
Author(s):  
Sha Gong ◽  
Yujie Wang ◽  
Wenbing Zhang
Keyword(s):  
Regulation Mechanism ◽  
Kinetic Regulation

scholarly journals Structural comparison of GLUT1 to GLUT3 reveal transport regulation mechanism in sugar porter family

2021 ◽  
Vol 4 (4) ◽  
pp. e202000858
Author(s):  
Tânia Filipa Custódio ◽  
Peter Aasted Paulsen ◽  
Kelly May Frain ◽  
Bjørn Panyella Pedersen
Keyword(s):  
Binding Site ◽  
Functional Data ◽  
Physiological Function ◽  
Regulation Mechanism ◽  
Sequence Motif ◽  
Open Conformation ◽  
Transport Regulation ◽  
Glucose Binding ◽  
The Difference ◽  
Kinetic Regulation

The human glucose transporters GLUT1 and GLUT3 have a central role in glucose uptake as canonical members of the Sugar Porter (SP) family. GLUT1 and GLUT3 share a fully conserved substrate-binding site with identical substrate coordination, but differ significantly in transport affinity in line with their physiological function. Here, we present a 2.4 Å crystal structure of GLUT1 in an inward open conformation and compare it with GLUT3 using both structural and functional data. Our work shows that interactions between a cytosolic “SP motif” and a conserved “A motif” stabilize the outward conformational state and increases substrate apparent affinity. Furthermore, we identify a previously undescribed Cl− ion site in GLUT1 and an endofacial lipid/glucose binding site which modulate GLUT kinetics. The results provide a possible explanation for the difference between GLUT1 and GLUT3 glucose affinity, imply a general model for the kinetic regulation in GLUTs and suggest a physiological function for the defining SP sequence motif in the SP family.

scholarly journals Structural comparison of GLUT1 to GLUT3 reveal transport regulation mechanism in Sugar Porter family

2020 ◽  
Author(s):  
Tânia Filipa Custódio ◽  
Peter Aasted Paulsen ◽  
Kelly May Frain ◽  
Bjørn Panyella Pedersen
Keyword(s):  
Binding Site ◽  
Functional Data ◽  
Physiological Function ◽  
Regulation Mechanism ◽  
Sequence Motif ◽  
Open Conformation ◽  
Glucose Binding ◽  
The Difference ◽  
Substrate Affinities ◽  
Kinetic Regulation

AbstractThe human glucose transporters GLUT1 and GLUT3 have a central role in glucose uptake as canonical members of the Sugar Porter (SP) family. GLUT1 and GLUT3 share a fully conserved substrate-binding site with identical substrate coordination, but differ significantly in transport affinity in line with their physiological function. Here we present a 2.4 Å crystal structure of GLUT1 in an inward open conformation and compare it with GLUT3 using both structural and functional data. Our work shows that interactions between a cytosolic “Sugar Porter motif” and a conserved “A motif” stabilize the outward conformational state and increases substrate apparent affinity. Furthermore, we identify a previously undescribed Cl- ion site in GLUT1 and an endofacial lipid/glucose binding site which modulate GLUT kinetics. The results provide a possible explanation for the difference between GLUT1 and GLUT3 glucose affinity, imply a general model for the kinetic regulation in GLUTs and suggest a physiological function for the defining SP sequence motif in the Sugar Porter family.Summary BlurbNew structure of GLUT1 compared to GLUT3 explain different substrate affinities. The result provide a functional rationale for key structural motifs that define the universal Sugar Porter family.

Role of 4-O Galloylchlorogenic Acid in Lung Cancer- An Insilico Approach

2017 ◽  
Vol 9 (5) ◽  
Author(s):  
Jaynthy C. ◽  
N. Premjanu ◽  
Abhinav Srivastava
Keyword(s):  
Lung Cancer ◽  
Cell Proliferation ◽  
In Silico ◽  
Computational Study ◽  
Regulation Mechanism ◽  
Down Regulation ◽  
Fruit Extract ◽  
In Vitro Techniques ◽  
Discovery Studio

Cancer is a major disease with millions of patients diagnosed each year with high mortality around the world. Various studies are still going on to study the further mechanisms and pathways of the cancer cell proliferation. Fucosylation is one of the most important oligosaccharide modifications involved in cancer and inflammation. In cancer development increased core fucosylation by FUT8 play an important role in cell proliferation. Down regulation of FUT8 expression may help cure lung cancer. Therefore the computational study based on the down regulation mechanism of FUT8 was mechanised. Sapota fruit extract, containing 4-Ogalloylchlorogenic acid was used as the inhibitor against FUT-8 as target and docking was performed using in-silico tool, Accelrys Discovery Studio. There were several conformations of the docked result, and conformation 1 showed 80% dock score between the ligand and the target. Further the amino acids of the inhibitor involved in docking were studied using another tool, Ligplot. Thus, in-silico analysis based on drug designing parameters shows that the fruit extract can be studied further using in-vitro techniques to know its pharmacokinetics.

MECHANISM OF FISCHAL REGULATION OF FORESTRY

2018 ◽  
pp. 67-72
Author(s):  
Igor Lytsur ◽  
Anatoliy Karpuk
Keyword(s):  
Fiscal Policy ◽  
Conceptual Framework ◽  
International Experience ◽  
Nature Management ◽  
Modern State ◽  
Regulation Mechanism ◽  
Balanced Development

The modern state and ways of features of fiscal regulation mechanism of forestry is investigated. Scientific-theoretical principles of its effect to provision of balanced development of forestry in the system of nature management fiscal policy are justified. Conceptual framework of fiscal regulation mechanism, taking into consideration international experience functioning is examined.

Regulation mechanism of irrigation schedule on population photosynthesis of winter wheat

2012 ◽  
Vol 20 (2) ◽  
pp. 189-196
Author(s):  
Li-Ping LIU ◽  
Zhu OUYANG ◽  
Lan-Fang WU ◽  
Zhen-Zhong SUN ◽  
Fa-Dong LI
Keyword(s):  
Winter Wheat ◽  
Irrigation Schedule ◽  
Regulation Mechanism

SUV39H1-Mediated DNMT1 is Participated in the Epigenetic Regulation of Smad3 in Cervical Cancer

2020 ◽  
Vol 20 ◽  
Author(s):  
Li Zhang ◽  
Sijuan Tian ◽  
Minyi Zhao ◽  
Ting Yang ◽  
Shimin Quan ◽  
...  
Keyword(s):  
Cervical Cancer ◽  
Cell Lines ◽  
Epigenetic Regulation ◽  
Promoter Region ◽  
Methylation Status ◽  
Regulation Mechanism ◽  
Methylation Specific Pcr ◽  
Specific Pcr ◽  
Immune Factor ◽  
Cancer Tissues

Background: Smad3 is a pivotal intracellular mediator for participating in the activation of multiple immune signal pathway. Objective: The epigenetic regulation mechanism of the positive immune factor Smad3 in cervical cancer remains unknown. Therefore, the epigenetic regulation on Smad3 is investigated in this study. Methods: The methylation status of SMAD3 was detected by Methylation-specific PCR (MS-PCR) and Quantitative Methylation-specific PCR (MS-qPCR) in cervical cancer tissues and cell lines. The underlying molecular mechanisms of SUV39H1-DNMT1-Smad3 regulation was elucidated using cervical cancer cell lines containing siRNA or/and overexpression system. Confirmation of the regulation of DNMT1 by SUV39H1 used Chromatin immunoprecipitation-qPCR (ChIP-qPCR). The statistical methods used for comparing samples between groups were paired t tests and one-way ANOVAs. Results: H3K9me3 protein which regulated by SUV39H1 directly interacts with the DNMT1 promoter region to regulate its expression in cervical cancer cells, resulting in the reduce expression of the downstream target gene DNMT1. In addition, DNMT1 mediates the epigenetic modulation of the SMAD3 gene by directly binding to its promoter region. The depletion of DNMT1 effectively restores the expression of Smad3 in vitro. Moreover, in an in vivo assay, the expression profile of SUV39H1-DNMT1 was found to correlate with Smad3 expression in accordance with the expression at the cellular level. Notably, the promoter region of SMAD3 was hypermethylated in cervical cancer tissues, and this hypermethylation inhibits the subsequent gene expression. Conclusion: These results indicate that SUV39H1-DNMT1 is a crucial Smad3 regulatory axis in cervical cancer. SUV39H1-DNMT1 axis may provide a potential therapeutic target for the treatment of cervical cancer.

Sign in / Sign up

Export Citation Format

Share Document