vma8p-gfp fusions can be functionally incorporated into v-atpase, suggesting structural flexibility at the top of v1可以功能纳入v-atpase vma8p-gfp融合,提出结构灵活性v1的顶部.pdfVIP
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vma8p-gfp fusions can be functionally incorporated into v-atpase, suggesting structural flexibility at the top of v1可以功能纳入v-atpase vma8p-gfp融合,提出结构灵活性v1的顶部
Int. J. Mol. Sci. 2011, 12, 4693-4704; doi:10.3390/ijm
OPEN ACCESS
International Journal of
Molecular Sciences
ISSN 1422-0067
/journal/ijms
Article
Vma8p-GFP Fusions Can Be Functionally Incorporated into
V-ATPase, Suggesting Structural Flexibility at the Top of V1
Szczepan Nowakowski, Dalibor Mijaljica, Mark Prescott and Rodney J. Devenish *
Department of Biochemistry and Molecular Biology, and ARC Centre of Excellence in Structural and
Functional Microbial Genomics, Monash University, Clayton campus, Victoria 3800, Australia;
E-Mails: szczepan.nowakowski@.au (S.N.); Dalibor.Mijaljica@ (D.M.);
Mark.Prescott@ (M.P.)
* Author to whom correspondence should be addressed; E-Mail: Rod.Devenish@;
Tel.: +61-3-9905-3782; Fax: +61-3-9902-9500.
Received: 7 June 2011; in revised form: 4 July 2011 / Accepted: 13 July 2011 /
Published: 20 July 2011
Abstract: The vacuolar ATPase (V-ATPase) complex of yeast (Saccharomyces cerevisiae)
is comprised of two sectors, V (catalytic) and V (proton transfer). The hexameric (A B )
1 O 3 3
cylinder of V has a central cavity that must accommodate at least part of the rotary stalk of
1
V-ATPase, a key component of which is subunit D (Vma8p). Recent electron microscopy
(EM) data for the prokaryote V-ATPase complex (Thermus thermophilus) suggest that
subunit D penetrates deeply
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