Sequence and over-expression of subunits of adenosine triphosphate synthase in thermophilic bacterium PS3

Ohta, Shigeo; Yohda, Masafumi; Ishizuka, Morio; Hirata, Hajime; Hamamoto, Toshiro; Otawara-Hamamoto, Yoko; Matsuda, Kakuko; Kagawa, Yasuo

doi:10.1016/0005-2728(88)90064-3

Cited by 144 publications

(88 citation statements)

References 26 publications

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“…The protein bands in gels were stained with Coomassie Brilliant Blue R-250. N-terminal amino acid sequencing was performed as described previously (50) and confirmed that both ␦ and ⑀ subunits had the same N-terminal amino acid sequences, starting with the N-terminal methionines, as those of subunits contained in the authentic TF 1 (51).…”

Section: Measurement Of Tnp-atp Binding Monitored By Fluorescentmentioning

confidence: 77%

Thermophilic F1-ATPase Is Activated without Dissociation of an Endogenous Inhibitor, ε Subunit

Kato

Matsui²,

Tanaka

et al. 1997

Journal of Biological Chemistry

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of thermophilic F 1 -ATPase were prepared, and their catalytic properties were compared to know the role of ␦ and ⑀ subunits in catalysis. The presence of ␦ subunit in the complexes had slight inhibitory effect on the ATPase activity. The effect of ⑀ subunit was more profound. The (؊⑀) complexes, ␣ 3 ␤ 3 ␥ and ␣ 3 ␤ 3 ␥␦, initiated ATP hydrolysis without a lag. In contrast, the (؉⑀) complexes, ␣ 3 ␤ 3 ␥⑀ and ␣ 3 ␤ 3 ␥␦⑀, started hydrolysis of ATP (<700 M) with a lag phase that was gradually activated during catalytic turnover. As ATP concentration increased, the lag phase of the (؉⑀) complexes became shorter, and it was not observed above 1 mM ATP. Analysis of binding and hydrolysis of the ATP analog, 2 ,3 -O-(2,4,6-trinitrophenyl)-ATP, suggested that the (؉⑀) complexes bound substrate only slowly. Differing from Escherichia coli F 1 -ATPase, the activation of the (؉⑀) complexes from the lag phase was not due to dissociation of ⑀ subunit since the re-isolated activated complex retained ⑀ subunit. This indicates that there are two alternative forms of the (؉⑀) complex, inhibited form and activated form, and the inhibited one is converted to the activated one during catalytic turnover.

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Section: Measurement Of Tnp-atp Binding Monitored By Fluorescentmentioning

confidence: 77%

Thermophilic F1-ATPase Is Activated without Dissociation of an Endogenous Inhibitor, ε Subunit

Kato

Matsui²,

Tanaka

et al. 1997

Journal of Biological Chemistry

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“…All regions obtained from PCR-amplification in the present study were verified by nucleotide sequencing. The resulting plasmid (named pTR19-ASDS⌬a) was used for transformation of the F 1 F 0 -deficient E. coli strain, DK8 (34). Culture of the recombinant strain (DK8/pTR19-ASDS⌬a) and preparation of inverted membrane vesicles were performed as described previously (20).…”

Section: Methodsmentioning

confidence: 99%

ATP Synthase that Lacks F0a-Subunit

Ono

Sone

Yoshida

et al. 2004

Journal of Biological Chemistry

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“…Both P. modestum and thermophilic Bacillus PS3 have a typical bacterial unc operon with nine genes in the order of uncIBEFHAGDC (26,27). The hybrid F 1 F o , composed of Bacillus PS3 F 1 and P. modestum F o , was generated by connecting P. modestum uncIBEFЈ and Bacillus PS3 uncFЈHAGDC.…”

Section: Hybrid F1fomentioning

confidence: 99%

The product of uncI gene in F ₁ F _o -ATP synthase operon plays a chaperone-like role to assist c -ring assembly

Suzuki

Ozaki

Sone³

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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Bacterial operons for F1Fo-ATP synthase typically include an uncI gene that encodes a function-unknown small hydrophobic protein.When we expressed a hybrid F 1Fo (F1 from thermophilic Bacillus PS3 and Na ؉ -translocating Fo from Propionigenium modestum) in Escherchia coli cells, we found that uncI derived from P. modestum was indispensable to produce active enzyme; without uncI, csubunits in F 1Fo existed as monomers but not as functional c11-ring. When uncI was expressed from another plasmid at the same time, active F 1Fo with c11-ring was produced. A plasmid containing only uncI and c-subunit gene produced c 11-ring, but a plasmid containing only c-subunit gene did not. Direct interaction of UncI protein with c-subunits was suggested from copurification of His-tagged UncI protein and c-subunits, both in the state of c 11-ring and c-monomers. Na ؉ induced dissociation of His-tagged UncI protein from c 11-ring but not from c-monomers. These results show that UncI is a chaperone-like protein that assists c 11-ring assembly from c-monomers in the membrane.protein folding ͉ membrane protein ͉ Na ϩ transport

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Sequence and over-expression of subunits of adenosine triphosphate synthase in thermophilic bacterium PS3

Cited by 144 publications

References 26 publications

Thermophilic F1-ATPase Is Activated without Dissociation of an Endogenous Inhibitor, ε Subunit

Thermophilic F1-ATPase Is Activated without Dissociation of an Endogenous Inhibitor, ε Subunit

ATP Synthase that Lacks F0a-Subunit

The product of uncI gene in F ₁ F _o -ATP synthase operon plays a chaperone-like role to assist c -ring assembly

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Sequence and over-expression of subunits of adenosine triphosphate synthase in thermophilic bacterium PS3

Cited by 144 publications

References 26 publications

Thermophilic F1-ATPase Is Activated without Dissociation of an Endogenous Inhibitor, ε Subunit

Thermophilic F1-ATPase Is Activated without Dissociation of an Endogenous Inhibitor, ε Subunit

ATP Synthase that Lacks F0a-Subunit

The product of uncI gene in F 1 F o -ATP synthase operon plays a chaperone-like role to assist c -ring assembly

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The product of uncI gene in F ₁ F _o -ATP synthase operon plays a chaperone-like role to assist c -ring assembly