Cellular Functions, Mechanism of Action, and Regulation of FTSH Protease

Ito, Koreaki; Akiyama, Yoshinori

doi:10.1146/annurev.micro.59.030804.121316

Cited by 366 publications

(355 citation statements)

References 101 publications

Supporting

Mentioning

341

Contrasting

Unclassified

Order By: Relevance

“…The ATPase domain includes the conserved Walker A, Walker B and second region of homology (SRH) motifs. The protease domain contains a zinc-binding motif, which is consistent with the finding that its proteolytic activity is stimulated by a zinc ion (Ito & &Akiyama, 2005).…”

Section: Introductionsupporting

confidence: 86%

Structural studies onHelicobacter pyloriATP-dependent protease, FtsH

Kim

Kang

Song

et al. 2008

J Synchrotron Radiat

View full text Add to dashboard Cite

The ATP-dependent protease, FtsH, degrades misassembled membrane proteins for quality control like SecY, subunit a of FoF1-ATPase, and YccA, and digests short-lived soluble proteins in order to control their cellular regulation, including 32, LpxC and cII. The FtsH protein has an N-terminal transmembrane segment and a large cytosolic region that consists of two domains, an ATPase and a protease domain. To provide a structural basis for the nucleotide-dependent domain motions and a better understanding of substrate translocation, the crystal structures of the Helicobacter pylori (Hp) FtsH ATPase domain in the nucleotide-free state and complexed with ADP, were determined. Two different structures of HpFtsH ATPase were observed, with the nucleotide-free state in an asymmetric unit, and these structures reveal the new forms and show other conformational differences between the nucleotidefree and ADP-bound state compared with previous structures. In particular, one HpFtsH Apo structure has a considerable rotation difference compared with the HpFtsH ADP complex, and this large conformational change reveals that FtsH may have the mechanical force needed for substrate translocation.

show abstract

Section: Introductionsupporting

confidence: 86%

Structural studies onHelicobacter pyloriATP-dependent protease, FtsH

Kim

Kang

Song

et al. 2008

J Synchrotron Radiat

View full text Add to dashboard Cite

show abstract

“…The ftsh gene encoding the FtsH protease was first described with E.coli [51][52][53]. The gene encodes a 71 kDa polypeptide, and its homologs have been identified in other bacteria, cyanobacteria and mitochondria, and chloroplasts of eukaryotes [54][55][56]. In E.coli, FtsH has been shown to be involved in the degradation of the heat shock transcription factor σ 32 FtsH belongs to the family of zinc metalloprotease.…”

Section: Molecular Structure and General Function Of Ftsh Proteasesmentioning

confidence: 99%

“…In E.coli, FtsH has been shown to be involved in the degradation of the heat shock transcription factor σ 32 FtsH belongs to the family of zinc metalloprotease. The arginine residue at the C-terminus of the SRH motif, the so-called 'arginine finger', is crucial for ATP hydrolysis [54,62]. The AAA family proteins assemble into oligomers, often hexamers, and form a ring-shaped structure with a central pore that has the catalytic site.…”

Section: Molecular Structure and General Function Of Ftsh Proteasesmentioning

confidence: 99%

Quality control of Photosystem II: The molecular basis for the action of FtsH protease and the dynamics of the thylakoid membranes

Yoshioka-Nishimura

Yamamoto

2014

Journal of Photochemistry and Photobiology B: Biology

View full text Add to dashboard Cite

The reaction center-binding D1 protein of Photosystem II is damaged by excessive light, which leads to photoinhibition of Photosystem II. The damaged D1 protein is removed immediately by specific proteases, and a metalloprotease FtsH located in the thylakoid membranes is involved in the proteolytic process. According to recent studies on the distribution and organization of the protein complexes/supercomplexes in the thylakoid membranes, the grana of higher plant chloroplasts are crowded with Photosystem II complexes and light-harvesting complexes. For the repair of the photodamaged D1 protein, the majority of the active hexameric FtsH proteases should be localized in close proximity to the Photosystem II complexes. The unstacking of the grana may increase the area of the grana margin and facilitate easier access of the FtsH proteases to the damaged D1 protein. These results suggest that the structural changes of the thylakoid membranes by light stress increase the mobility of the membrane proteins and support the quality control of Photosystem II. (159 words)

show abstract

“…Interaction candidate HtpX and the FtsH holo-complex consisting of FtsH, HflC, and HflK are the major proteases responsible for the turnover of integral inner membrane proteins in bacteria. 48 It is conceivable that these proteases are also involved in the quality control of the T3SS needle complex.…”

Section: Saint-wy Yields More Interaction Candidates Than Tspm-wy Tsmentioning

confidence: 99%

Pre- and Post-Processing Workflow for Affinity Purification Mass Spectrometry Data

et al. 2014

View full text Add to dashboard Cite

The reliable detection of protein-protein interactions by affinity purification mass spectrometry (AP-MS) is crucial for the understanding of biological processes. Quantitative information can be used to separate truly interacting proteins from false positives by contrasting counts of proteins binding to specific baits with counts of negative controls.Several approaches have been proposed for computing scores for potential interaction proteins, e.g. the commonly used SAINT software. However, it remains a subjective decision where to set the cutoff score for candidate selection and, further, no precise control for the expected number of false positives is provided.In related fields, successful data analysis strongly relies on statistical pre-and postprocessing steps which, so far, have only played a minor role in AP-MS data analysis. We introduce a complete workflow, embedding either the scoring method SAINT or alternatively a two-stage-poisson model into a pre-and postprocessing framework. To this end, we investigate different normalization methods and apply a statistical filter adjusted to AP-MS data. Further, we propose permutation and adjustment procedures, which allow the replacement of scores by statistical p-values.

show abstract

Cellular Functions, Mechanism of Action, and Regulation of FTSH Protease

Cited by 366 publications

References 101 publications

Structural studies onHelicobacter pyloriATP-dependent protease, FtsH

Structural studies onHelicobacter pyloriATP-dependent protease, FtsH

Quality control of Photosystem II: The molecular basis for the action of FtsH protease and the dynamics of the thylakoid membranes

Pre- and Post-Processing Workflow for Affinity Purification Mass Spectrometry Data

Contact Info

Product

Resources

About