scholarly journals Refinement of the Central Steps of Substrate Transport by the Aspartate Transporter GltPh: Elucidating the Role of the Na2 Sodium Binding Site

2015 ◽  
Vol 11 (10) ◽  
pp. e1004551 ◽  
Author(s):  
SanthoshKannan Venkatesan ◽  
Kusumika Saha ◽  
Azmat Sohail ◽  
Walter Sandtner ◽  
Michael Freissmuth ◽  
...  
Biochemistry ◽  
2000 ◽  
Vol 39 (7) ◽  
pp. 1817-1825 ◽  
Author(s):  
Alireza R. Rezaie ◽  
Xuhua He

Diabetes ◽  
1997 ◽  
Vol 46 (3) ◽  
pp. 354-362 ◽  
Author(s):  
K. Matsuda ◽  
E. Araki ◽  
R. Yoshimura ◽  
K. Tsuruzoe ◽  
N. Furukawa ◽  
...  

Genetics ◽  
1991 ◽  
Vol 128 (1) ◽  
pp. 45-57 ◽  
Author(s):  
C T Kuan ◽  
S K Liu ◽  
I Tessman

Abstract Excision and transposition of the Tn5 element in Escherichia coli ordinarily appear to occur by recA-independent mechanisms. However, recA(Prtc) genes, which encode RecA proteins that are constitutively activated to the protease state, greatly enhanced excision and transposition; both events appeared to occur concomitantly and without destruction of the donor DNA. The recombinase function of the RecA protein was not required. Transposition was accompanied by partial, and occasionally full, restoration of the functional integrity of the gene vacated by the excised Tn5. The stimulation of transposition was inhibited by an uncleavable LexA protein and was strongly enhanced by an additional role of the RecA(Prtc) protein besides its mediation of LexA cleavage. To account for the enhanced transposition, we suggest that (i) there may be a LexA binding site within the promoter for the IS50 transposase, (ii) activated RecA may cleave the IS50 transposition inhibitor, and (iii) the transposase may be formed by RecA cleavage of a precursor molecule.


2021 ◽  
Vol 22 (7) ◽  
pp. 3572
Author(s):  
Jeff Abramson ◽  
Ernest M. Wright

Active transport of sugars into bacteria occurs through symporters driven by ion gradients. LacY is the most well-studied proton sugar symporter, whereas vSGLT is the most characterized sodium sugar symporter. These are members of the major facilitator (MFS) and the amino acid-Polyamine organocation (APS) transporter superfamilies. While there is no structural homology between these transporters, they operate by a similar mechanism. They are nano-machines driven by their respective ion electrochemical potential gradients across the membrane. LacY has 12 transmembrane helices (TMs) organized in two 6-TM bundles, each containing two 3-helix TM repeats. vSGLT has a core structure of 10 TM helices organized in two inverted repeats (TM 1–5 and TM 6–10). In each case, a single sugar is bound in a central cavity and sugar selectivity is determined by hydrogen- and hydrophobic- bonding with side chains in the binding site. In vSGLT, the sodium-binding site is formed through coordination with carbonyl- and hydroxyl-oxygens from neighboring side chains, whereas in LacY the proton (H3O+) site is thought to be a single glutamate residue (Glu325). The remaining challenge for both transporters is to determine how ion electrochemical potential gradients drive uphill sugar transport.


FEBS Letters ◽  
2006 ◽  
Vol 580 (3) ◽  
pp. 912-917 ◽  
Author(s):  
Jiro Arima ◽  
Yoshiko Uesugi ◽  
Misugi Uraji ◽  
Masaki Iwabuchi ◽  
Tadashi Hatanaka

2018 ◽  
Vol 98 ◽  
pp. 15-24 ◽  
Author(s):  
Guadalupe del C. Pizarro ◽  
Oscar G. Marambio ◽  
Manuel Jeria-Orell ◽  
Diego P. Oyarzún ◽  
Julio Sánchez

Endocrinology ◽  
1986 ◽  
Vol 118 (3) ◽  
pp. 990-998 ◽  
Author(s):  
VENKAT GOPALAKRISHNAN ◽  
CHRIS R. TRIGGLE ◽  
PRAKASH V. SULAKHE ◽  
J. ROBERT McNEILL

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