The Escherichia coli FtsH protein is a prokaryotic member of a protein family of putative ATPases involved in membrane functions, cell cycle control, and gene expression

Tomoyasu, Toshifumi; Yuki, T.; Morimura, Shigeru; Mori, Hirotada; Yamanaka, Kunitoshi; Niki, Hironori; Hiraga, Sota; Ogura, Teru

doi:10.1128/jb.175.5.1344-1351.1993

Cited by 225 publications

(194 citation statements)

References 32 publications

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“…For example, loss of an m-AAA protease in human mitochondria has been shown to cause a severe illness (Casari et al, 1998). The deletion of ftsH is lethal in E. coli (Tomoyasu et al, 1993) and causes a severe growth defect in Bacillus subtilis (Deuerling et al, 1997). Similarly, leaf variegation appears as a typical phenotype of FtsH deficiency in higher plants (Sakamoto, 2003).…”

Section: Leaf Variegation and Inactivation Of The Ftsh Gene Familymentioning

confidence: 99%

Coordinated Regulation and Complex Formation of YELLOW VARIEGATED1 and YELLOW VARIEGATED2, Chloroplastic FtsH Metalloproteases Involved in the Repair Cycle of Photosystem II in Arabidopsis Thylakoid Membranes

et al. 2003

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Arabidopsis YELLOW VARIEGATED1 ( VAR1 ) and VAR2 are separate loci that encode similar chloroplast FtsH proteases. To date, FtsH is the best-characterized protease in thylakoid membranes involved in the turnover of photosynthetic protein complexes. It comprises a protein family that is encoded by 12 different nuclear genes in Arabidopsis. We show here that nine FtsH proteins are located in the chloroplasts. Mutations in either VAR1 or VAR2 cause typical leaf variegation and sensitivity to photoinhibition. By contrast, none of these phenotypes was observed in T-DNA insertion mutants in other ftsH genes ( ftsh1 , ftsh6 , and ftsh8 ) closely related to VAR1 and VAR2 . This finding suggests that VAR1 and VAR2 play a predominant role in the photosystem II repair cycle in thylakoid membranes. By generating VAR1-and VAR2-specific antibodies, we found that loss of either VAR1 or VAR2 results in the decreased accumulation of the other. Thus, the genetic nonredundancy between VAR1 and VAR2 could be attributed to their coordinated regulation at the protein level. These observations led us to examine whether VAR1 and VAR2 form a complex. Sucrose density gradient and gel filtration analyses revealed a complex of ‫ف‬ 400 to 450 kD, probably representing a hexamer. Furthermore, VAR1 and VAR2 were shown to coprecipitate by immunoprecipitation using VAR1-and VAR2-specific antibodies. The majority of VAR1 appears to exist as heterocomplexes with VAR2, whereas VAR2 may be present as homocomplexes as well. Based on these results, we conclude that VAR1 and VAR2 are the major components of an FtsH complex involved in the repair of photodamaged proteins in thylakoid membranes.

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Section: Leaf Variegation and Inactivation Of The Ftsh Gene Familymentioning

confidence: 99%

Coordinated Regulation and Complex Formation of YELLOW VARIEGATED1 and YELLOW VARIEGATED2, Chloroplastic FtsH Metalloproteases Involved in the Repair Cycle of Photosystem II in Arabidopsis Thylakoid Membranes

et al. 2003

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“…Dom I and // denote the two ATPase domains. Walker A and B motifs and the 'second region of homology' as defined in [9] are marked. Above the alignment is given the consensus secondary structure for the two ATPase domains (open bars denote a-helices and arrows P-strands).…”

Section: Assay For Atpase Activitymentioning

confidence: 99%

“…Recently, a new family of P-loop NTPases has emerged, the AAA family (for ATPases Associated with a variety of cellular Activities) [7], some of whose best known members are the ATPase subunits of the 26S proteasome [8], FtsH [9], and NSF [10]. The hallmark of these proteins is a highly conserved domain of approximately 250 residues, which contains a second region of high sequence conservation C-terminal to the ATP-binding motifs.…”

Section: Introductionmentioning

confidence: 99%

Cloning, sequencing and expression of VAT, a CDC48/p97 ATPase homologue from the archaeon Thermoplasma acidophilum

et al. 1997

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A member of the AAA family of Mg + -ATPases from the archaeon Thermoplasma acidophilum has been cloned and expressed in Escherichia coli. The protein, VCP-like ATPase of Thermoplasma acidophilum (VAT), is a homologue of SAV from Sulfolobus acidocaldarius and CdcH of Halobacterium salinarium, and belongs to the CDC48/VCP/p97 subfamily. The deduced product of the vat gene is 745 residues long (M r 83 000), which has an optimal Mg 2+ -ATPase activity at 70°C. Electron microscopy shows the purified protein to form single and double homo-hexameric rings. Although the symmetry is different, the appearance of the complexes formed of two rings resembles the 20S proteasome and Hsp60/GroEL.

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“…neutral, zinc-dependent protease Campbell et al, 1994). Ymelp is closely related to the Escherichia coli protein FtsH, which was identified in a screen for cell division mutants (Tomoyasu et al, 1993b). Both Ymelp and FtsH contain a putative ATPase domain and the zinc-dependent protease element.…”

Section: Introductionmentioning

confidence: 99%

Biochemical and functional analysis of the YME1 gene product, an ATP and zinc-dependent mitochondrial protease from S. cerevisiae.

Weber

Hanekamp

Thorsness

1996

MBoC

129

106

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Inactivation of YME1 in yeast causes several distinct phenotypes: an increased rate of DNA escape from mitochondria, temperature-sensitive growth on nonfermentable carbon sources, extremely slow growth when mitochondrial DNA is completely absent from the cell, and altered morphology of the mitochondrial compartment. The protein encoded by YME1, Ymelp, contains two highly conserved sequence elements, one implicated in the binding and hydrolysis of ATP, and the second characteristic of active site residues found in neutral, zinc-dependent proteases. Both the putative ATPase and zinc-dependent protease elements are necessary for the function of Ymelp as genes having mutations in critical residues of either of these motifs are unable to suppress any of the phenotypes exhibited by ymel deletion strains. Ymelp co-fractionates with proteins associated with the mitochondrial inner membrane, is tightly associated with this membrane, and is oriented with the bulk of the protein facing the matrix. Unassembled subunit II of cytochrome oxidase is stabilized in ymel yeast strains. The data support a model in which Ymelp is an ATP and zinc-dependent protease associated with the matrix side of the inner mitochondrial membrane. Subunit II of cytochrome oxidase, when not assembled into a higher order complex, is a likely substrate of Ymelp.

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The Escherichia coli FtsH protein is a prokaryotic member of a protein family of putative ATPases involved in membrane functions, cell cycle control, and gene expression

Cited by 225 publications

References 32 publications

Coordinated Regulation and Complex Formation of YELLOW VARIEGATED1 and YELLOW VARIEGATED2, Chloroplastic FtsH Metalloproteases Involved in the Repair Cycle of Photosystem II in Arabidopsis Thylakoid Membranes

Coordinated Regulation and Complex Formation of YELLOW VARIEGATED1 and YELLOW VARIEGATED2, Chloroplastic FtsH Metalloproteases Involved in the Repair Cycle of Photosystem II in Arabidopsis Thylakoid Membranes

Cloning, sequencing and expression of VAT, a CDC48/p97 ATPase homologue from the archaeon Thermoplasma acidophilum

Biochemical and functional analysis of the YME1 gene product, an ATP and zinc-dependent mitochondrial protease from S. cerevisiae.

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