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Cytosolic region of TM6 in P-glycoprotein: topographical analysis and functional perturbation by site directed labeling.

Abstract：

:Reduced intracellular drug accumulation due to the activity of the drug efflux pump ABC (B1) is a major mechanism in the resistance of cancer cells to chemotherapy. ABC (B1) is a poly specific transporter, and the molecular mechanism of its complex translocation process remains to be elucidated. To understand the process will require information on the regions involved in drug binding and those that couple this event to nucleotide hydrolysis. The present investigation focuses on the cytosolic region of transmembrane helix 6 (TM6), which has been widely attributed with a central role in the translocation process. A series of ABC (B1) isoforms containing a unique cysteine within TM6 was constructed and the resultant proteins purified and reconstituted. Accessibility of the cysteines to covalent modification by maleimide reagents was measured for the basal, ATP bound and vanadate trapped conformations of each isoform. Residues at the two extremes of the TM6 region examined (amino acids 344 to 360) were considerably more accessible than the central segment, the latter of which also failed to undergo significant conformational changes during the catalytic cycle. Covalent modification of the cytosolic segment of TM6 did, however, attenuate drug stimulation of ATP hydrolysis and demonstrates an important role for this segment in coupling drug binding to ATP hydrolysis during translocation.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Storm J,Modok S,O'Mara ML,Tieleman DP,Kerr ID,Callaghan R

doi

10.1021/bi7023089

subject

Has Abstract

pub_date

2008-03-25 00:00:00

pages

3615-24

issue

12

eissn

0006-2960

issn

1520-4995

journal_volume

47

pub_type

杂志文章

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