2005
DOI: 10.1016/j.febslet.2005.11.036
|View full text |Cite
|
Sign up to set email alerts
|

Isolated ε subunit of Bacillus subtilis F1‐ATPase binds ATP

Abstract: Previously, we demonstrated ATP binding to the isolated e subunit of F 1 -ATPase from thermophilic Bacillus PS3 [Kato-Yamada Y., Yoshida M. (2003) J. Biol. Chem. 278, 36013]. However, whether it is a general feature of the e subunit from other sources is yet unclear. Here, using a sensitive method to detect weak interactions between fluorescently labeled e subunit and nucleotide, it was shown that the e subunit of F 1 -ATPase from Bacillus subtilis also bound ATP. The dissociation constant for ATP binding at … Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1

Citation Types

5
26
0

Year Published

2007
2007
2020
2020

Publication Types

Select...
6
1
1

Relationship

1
7

Authors

Journals

citations
Cited by 39 publications
(31 citation statements)
references
References 25 publications
5
26
0
Order By: Relevance
“…This model is supported with the recent crystal structure of the Bacillus PS3 subunit ε with ATP associated to the C-terminus of this subunit [27]. In summary, these studies show that ε works as an ATP sensor in bacteria that posses a novel ATP-binding motif in this subunit [26][27][28][29].…”
Section: The Central Stalk Is Part Of the Atp Synthase Rotorsupporting
confidence: 69%
“…This model is supported with the recent crystal structure of the Bacillus PS3 subunit ε with ATP associated to the C-terminus of this subunit [27]. In summary, these studies show that ε works as an ATP sensor in bacteria that posses a novel ATP-binding motif in this subunit [26][27][28][29].…”
Section: The Central Stalk Is Part Of the Atp Synthase Rotorsupporting
confidence: 69%
“…The latter has a well-defined ATP-binding site with a sequence motif, I(L)DXXRA, that is conserved in most bacterial subunits. The ATP binding to EF 1 (this work) and to B. subtilis (34) support the proposed motif. An up-extended structural model was proposed based on the obtained conformations and the information reported so far.…”
supporting
confidence: 76%
“…The efficiency of the conversion to the down-state was regulated by the ATP concentration and membrane potential. Actually, the isolated subunits of TF 1 and Bacillus subtilis F 1 were found to bind ATP (33,34), suggesting the importance of ATP binding in regulation of the conformational change of . However, there have been no structural data on TF 1 so far.…”
mentioning
confidence: 99%
“…Subunit ε of E. coli has been shown to bind ATP, but the affinity is low (dissociation constant [K d ] ϭ 22 mM) (50). This is in contrast to obligate aerobes like Bacillus species, where the K d is in the range of 0.67 to 2.2 mM (17,19). Experiments have not been performed to determine a physiological role for subunit ε in the growth of Bacillus species and other obligate aerobes, and this is the focus of ongoing studies.…”
mentioning
confidence: 99%