scholarly journals Maltose-binding protein effectively stabilizes the partially closed conformation of the ATP-binding cassette transporter MalFGK2

2017 ◽  
Vol 19 (14) ◽  
pp. 9366-9373 ◽  
Author(s):  
Jingwei Weng ◽  
Shuo Gu ◽  
Xin Gao ◽  
Xuhui Huang ◽  
Wenning Wang
Keyword(s):  
Abc Transporter ◽  
Binding Protein ◽  
Maltose Binding Protein ◽  
Atp Binding ◽  
Type I ◽  
Closed Conformation ◽  
Atp Binding Cassette Transporter ◽  
Maltose Transporter ◽  
Atp Binding Cassette

Maltose transporter MalFGK2is a type-I importer in the ATP-binding cassette (ABC) transporter superfamily.

scholarly journals The MalF P2 Loop of the ATP-Binding Cassette Transporter MalFGK2 from Escherichia coli and Salmonella enterica Serovar Typhimurium Interacts with Maltose Binding Protein (MalE) throughout the Catalytic Cycle

2008 ◽  
Vol 191 (3) ◽  
pp. 754-761 ◽  
Author(s):  
Martin L. Daus ◽  
Mathias Grote ◽  
Erwin Schneider
Keyword(s):  
Escherichia Coli ◽  
Salmonella Enterica ◽  
Binding Protein ◽  
Maltose Binding Protein ◽  
Cross Linking ◽  
Atp Binding ◽  
Cross Link ◽  
Atp Binding Cassette Transporter ◽  
Serovar Typhimurium ◽  
Atp Binding Cassette

ABSTRACT We have investigated the interaction of the uncommonly large periplasmic P2 loop of the MalF subunit of the maltose ATP-binding cassette transporter (MalFGK2) from Escherichia coli and Salmonella enterica serovar Typhimurium with maltose binding protein (MalE) by site-specific chemical cross-linking in the assembled transport complex. We focused on possible distance changes between two pairs of residues of the P2 loop and MalE during the transport cycle. The distance between MalF(S205C) and MalE(T80C) (∼5 Å) remained unchanged under all conditions tested. Cross-linking did not affect the ATPase activity of the complex. The distance between MalF(T177C) and MalE(T31C) changed from ∼10 Å to ∼5 Å upon binding of ATP (or maltose, with a less pronounced result) and was reset to ∼10 Å after hydrolysis of one ATP. A cross-link (∼25 Å) between MalF(S205C) and MalE(T31C) was observed only when the transporter resided in a transition state-like conformation, as was the case after vanadate trapping or in a binding protein-independent mutant, both of which are characterized by tight binding of unliganded MalE to the transporter. Thus, we propose that the observed cross-link is indicative of catalytic intermediates of the transporter. Together, our results strengthen the notion that the MalF P2 loop plays an important role in intersubunit communication. In particular, this loop is involved in keeping MalE in close contact with the transporter. The data are discussed with respect to a crystal structure and current transport models.

scholarly journals Full engagement of liganded maltose-binding protein stabilizes a semi-open ATP-binding cassette dimer in the maltose transporter

2015 ◽  
Vol 98 (5) ◽  
pp. 878-894 ◽  
Author(s):  
Frances Joan D. Alvarez ◽  
Cédric Orelle ◽  
Yan Huang ◽  
Ruchika Bajaj ◽  
R. Michael Everly ◽  
...  
Keyword(s):  
Binding Protein ◽  
Maltose Binding Protein ◽  
Atp Binding ◽  
Maltose Transporter ◽  
Atp Binding Cassette

Periplasmic Loop P2 of the MalF Subunit of the Maltose ATP Binding Cassette Transporter Is Sufficient To Bind the Maltose Binding Protein MalE†

Biochemistry ◽  
2009 ◽  
Vol 48 (10) ◽  
pp. 2216-2225 ◽  
Author(s):  
Tomas Jacso ◽  
Mathias Grote ◽  
Martin L. Daus ◽  
Peter Schmieder ◽  
Sandro Keller ◽  
...  
Keyword(s):  
Binding Protein ◽  
Maltose Binding Protein ◽  
Atp Binding ◽  
Atp Binding Cassette Transporter ◽  
Atp Binding Cassette

scholarly journals ATP Binding Cassette Transporter A1 is Involved in Extracellular Secretion of Acetylated APE1/Ref-1

2019 ◽  
Vol 20 (13) ◽  
pp. 3178 ◽  
Author(s):  
Yu Ran Lee ◽  
Hee Kyoung Joo ◽  
Eun Ok Lee ◽  
Hyun Sil Cho ◽  
Sunga Choi ◽  
...  
Keyword(s):  
Abc Transporter ◽  
Abc Transporters ◽  
Secretory Pathway ◽  
Trichostatin A ◽  
Atp Binding ◽  
Terminal Protein ◽  
Secretion Signal ◽  
Extracellular Secretion ◽  
Atp Binding Cassette Transporter ◽  
Atp Binding Cassette

Acetylation of nuclear apurinic/apyrimidinic endonuclease-1/redox factor-1 (APE1/Ref-1) is associated with its extracellular secretion, despite the lack of an N-terminal protein secretion signal. In this study, we investigated plasma membrane targeting and translocation of APE1/Ref-1 in HEK293T cells with enhanced acetylation. While APE1/Ref-1 targeting was not affected by inhibition of the endoplasmic reticulum/Golgi-dependent secretion, its secretion was reduced by inhibitors of ATP-binding cassette (ABC) transporters, and siRNA-mediated down-regulation of ABC transporter A1. The association between APE1/Ref-1 and ABCA1 transporter was confirmed by proximal ligation assay and immunoprecipitation experiments. An APE1/Ref-1 construct with mutated acetylation sites (K6/K7R) showed reduced co-localization with ABC transporter A1. Exposure of trichostatin A (TSA) induced the acetylation of APE1/Ref-1, which translocated into membrane fraction. Taken together, acetylation of APE1/Ref-1 is considered to be necessary for its extracellular targeting via non-classical secretory pathway using the ABCA1 transporter.

Evidence for the presence of ATP-binding cassette transporter (ABC transporter) A1 in stallion spermatozoa

2012 ◽  
Vol 32 (8) ◽  
pp. 497 ◽  
Author(s):  
M. Merkl ◽  
S. Schäfer-Somi ◽  
I. Walter ◽  
M. Helmreich ◽  
M. Glösmann ◽  
...  
Keyword(s):  
Abc Transporter ◽  
Atp Binding ◽  
Atp Binding Cassette Transporter ◽  
Atp Binding Cassette

scholarly journals Effects of Astaxanthin on Reverse Cholesterol Transport and Atherosclerosis in Mice

2017 ◽  
Vol 2017 ◽  
pp. 1-6 ◽  
Author(s):  
Tang-Bin Zou ◽  
Shan-Shan Zhu ◽  
Fei Luo ◽  
Wei-Qiao Li ◽  
Xue-Rong Sun ◽  
...  
Keyword(s):  
Reverse Cholesterol Transport ◽  
Scavenger Receptor ◽  
Hdl Cholesterol ◽  
High Plasma ◽  
Cholesterol Transport ◽  
Atp Binding ◽  
Type I ◽  
Aortic Sinus ◽  
Atp Binding Cassette Transporter ◽  
Atp Binding Cassette

High plasma level of HDL-cholesterol (HDL-C) has been consistently associated with a decreased risk of atherosclerosis (AS); thus, HDL-C is considered to be an antiatherogenic lipoprotein. The development of novel therapies to enhance the atheroprotective properties of HDL may have the possibility of further reducing the residual AS risk. Reverse cholesterol transport (RCT) is believed to be a primary atheroprotective activity of HDL, which has been shown to promote the efflux of excess cholesterol from macrophage-derived foam cells via ATP-binding cassette transporter A1 (ABCA1), ATP-binding cassette transporter G1 (ABCG1), and scavenger receptor class B type I (SR-BI) and then transport it back to the liver for excretion into bile and eventually into the feces. In the current study, we investigated the effects of astaxanthin on RCT and AS progression in mice. The results showed that short- and long-term supplementation of astaxanthin promote RCT in C57BL/6J and ApoE−/−mice, respectively. Moreover, astaxanthin can relieve the plaque area of the aortic sinus and aortic cholesterol in mice. These findings suggest that astaxanthin is beneficial for boosting RCT and preventing the development of AS.

scholarly journals Exploring the Role of Integral Membrane Proteins in ATP-Binding Cassette Transporters: Analysis of a Collection of MalG Insertion Mutants

1998 ◽  
Vol 180 (9) ◽  
pp. 2507-2514 ◽  
Author(s):  
Bryn D. Nelson ◽  
Beth Traxler
Keyword(s):  
Membrane Proteins ◽  
Cytoplasmic Membrane ◽  
Binding Protein ◽  
Maltose Binding Protein ◽  
Integral Membrane Proteins ◽  
Atp Binding ◽  
Mutant Proteins ◽  
Transport Complex ◽  
Atp Binding Cassette

ABSTRACT The maltose transport complex of Escherichia coli is a well-studied example of an ATP-binding cassette transporter. The complex, containing one copy each of the integral membrane proteins MalG and MalF and two copies of the peripheral cytoplasmic membrane protein MalK, interacts with the periplasmic maltose-binding protein to efficiently translocate maltose and maltodextrins across the bacterial cytoplasmic membrane. To investigate the role of MalG both in MalFGK2 assembly interactions and in subsequent transport interactions, we isolated and characterized 18 different MalG mutants, each containing a 31-residue insertion in the protein. Eight insertions mapping to distinct hydrophilic regions of MalG permitted either assembly or both assembly and transport interactions to occur. In particular, we isolated two insertions mapping to extracytoplasmic (periplasmic) regions of MalG which preserved both assembly and transport abilities, suggesting that these are permissive sites in the protein. Another periplasmic insertion seems to affect only transport-specific interactions between MalG and maltose-binding protein, defining a novel class of MalG mutants. Finally, four MalG mutant proteins, although stably expressed, are unable to assemble into the MalFGK2 complex. These mutants contain insertions in only two different hydrophilic regions of MalG, consistent with the notion that a restricted number of domains in this protein are critical complex assembly determinants. These MalG mutants will allow us to further explore the intermolecular interactions of this model transporter.

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