The α-Subunit of Leishmania F1 ATP Synthase Hydrolyzes ATP in Presence of tRNA
IR@IICB: CSIR-Indian Institute of Chemical Biology, Kolkata
View Archive Info| Field | Value | |
| Title |
The α-Subunit of Leishmania F1 ATP Synthase Hydrolyzes ATP in Presence of tRNA
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| Creator |
Goswami, Srikanta
Adhya, Samit |
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| Subject |
Molecular & Human Genetics
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| Description |
Import of tRNAs into the mitochondria of the kinetoplastid
protozoon Leishmania requires the tRNA-dependent hydrolysis
of ATP leading to the generation of membrane potential
through the pumping of protons. Subunit RIC1 of the inner
membrane RNA import complex is a bi-functional protein that
is identical to the �-subunit of F1F0 ATP synthase and specifically binds to a subset (Type I) of importable tRNAs. We show that recombinant, purified RIC1 is a Type I tRNA-dependent ATP hydrolase. The activity was insensitive to oligomycin, sensitive to mutations within the import signal of the tRNA, and required the cooperative interaction between the ATP-binding and C-terminal domains of RIC1. The ATPase activity of the intact complex was inhibited by anti-RIC1 antibody, while knockdown of RIC1 in Leishmania tropica resulted in deficiency
of the tRNA-dependent ATPase activity of the mitochondrial
inner membrane. Moreover, RIC1 knockdown extracts
failed to generate a membrane potential across reconstituted
proteoliposomes, as shown by a rhodamine 123 uptake assay,
but activity was restored by adding back purified RIC1. These observations identify RIC1 as a novel form of the F1 ATP synthase �-subunit that acts as the major energy transducer fortRNA import.
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| Date |
2006
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| Type |
Article
PeerReviewed |
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| Format |
application/pdf
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| Identifier |
http://www.eprints.iicb.res.in/482/1/JOURNAL_OF_BIOLOGICAL_CHEMISTRY%2C__281(_28)%2C_18914%2D18917_[62].pdf
Goswami, Srikanta and Adhya, Samit (2006) The α-Subunit of Leishmania F1 ATP Synthase Hydrolyzes ATP in Presence of tRNA. THE JOURNAL OF BIOLOGICAL CHEMISTRY, 281 (28). pp. 18914-18917. |
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| Relation |
http://www.jbc.org/content/281/28/18914.full.pdf+html
http://www.eprints.iicb.res.in/482/ |
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