Proteolysis of the phage λ CII regulatory protein by FtsH (HflB) of <i>Escherichia coli</i>

Shotland, Yoram; Koby, Simi; Teff, Dinah; Mansur, Nora; Oren, Deena A.; Tatematsu, K.; Tomoyasu, Toshifumi; Kessel, Martin; Bukau, Bernd; Ogura, Teru; Oppenheim, Amos B.

doi:10.1046/j.1365-2958.1997.4231796.x

Cited by 133 publications

(126 citation statements)

References 41 publications

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“…Previous work has shown that E. coli FtsH can tolerate the addition of an affinity tag at the C terminus (Akiyama et al, 1995;Shotland et al, 1997). Consequently, to aid the purification of FtsH2, we constructed a strain of Synechocystis 6803, termed SynFtsH2GST, in which a GST affinity tag that also included a C-terminal Strep II tag, was fused to the C terminus of FtsH2 (see Methods).…”

Section: Phenotype Of a Gst-tagged Ftsh2 Derivative Of Synechocystis mentioning

confidence: 99%

Subunit Organization of a Synechocystis Hetero-Oligomeric Thylakoid FtsH Complex Involved in Photosystem II Repair

Boehm

Krynická

et al. 2012

The Plant Cell

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FtsH metalloproteases are key components of the photosystem II (PSII) repair cycle, which operates to maintain photosynthetic activity in the light. Despite their physiological importance, the structure and subunit composition of thylakoid FtsH complexes remain uncertain. Mutagenesis has previously revealed that the four FtsH homologs encoded by the cyanobacterium Synechocystis sp PCC 6803 are functionally different: FtsH1 and FtsH3 are required for cell viability, whereas FtsH2 and FtsH4 are dispensable. To gain insights into FtsH2, which is involved in selective D1 protein degradation during PSII repair, we used a strain of Synechocystis 6803 expressing a glutathione S-transferase (GST)-tagged derivative (FtsH2-GST) to isolate FtsH2-containing complexes. Biochemical analysis revealed that FtsH2-GST forms a hetero-oligomeric complex with FtsH3. FtsH2 also interacts with FtsH3 in the wild-type strain, and a mutant depleted in FtsH3, like ftsH2 2 mutants, displays impaired D1 degradation. FtsH3 also forms a separate heterocomplex with FtsH1, thus explaining why FtsH3 is more important than FtsH2 for cell viability. We investigated the structure of the isolated FtsH2-GST/FtsH3 complex using transmission electron microscopy and single-particle analysis. The three-dimensional structural model obtained at a resolution of 26 Å revealed that the complex is hexameric and consists of alternating FtsH2/FtsH3 subunits.

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Section: Phenotype Of a Gst-tagged Ftsh2 Derivative Of Synechocystis mentioning

confidence: 99%

Subunit Organization of a Synechocystis Hetero-Oligomeric Thylakoid FtsH Complex Involved in Photosystem II Repair

Boehm

Krynická

et al. 2012

The Plant Cell

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“…1c, d). FtsH contributes to the activation of the lytic cycle of phage l in E. coli by regulating the levels of the transcription factor CII and Xis (Shotland et al, 1997;Leffers & Gottesman, 1998). Thus, a probable scenario could be that TP712 gets locked in the lysogenic state in L. lactis DftsH because the ftsH mutation inhibits prophage activation or replication of the TP712 DNA.…”

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confidence: 99%

Lack of the host membrane protease FtsH hinders release of the Lactococcus lactis bacteriophage TP712

Roces

Wegmann

Campelo

et al. 2013

Journal of General Virology

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The temperate bacteriophage TP712 was unable to plaque on Lactococcus lactis DftsH lacking the membrane protease FtsH and complementation in trans restored the WT phenotype. Absence of ftsH did not hinder phage adsorption, phage DNA delivery or activation of the lytic cycle. Thin sections revealed that TP712 virions appeared to be correctly assembled inside the DftsH host, but were not released. These virions were infective, demonstrating that a functional host FtsH is required by TP712 to proceed effectively with lysis of the host.Large-scale dairy fermentations can be seriously compromised by bacteriophages infecting lactic acid bacteria (LAB), and particularly Lactococcus lactis, which is a commonly used starter culture for cheese making (Garneau & Moineau, 2011). Lactococcal phages are currently classified in 10 groups, eight of them belonging to the Siphoviridae family of the order Caudovirales. Those of the c2, 936 and P335 groups are the most commonly found in dairy plants (Deveau et al., 2006).A considerable effort has been made to improve and select phage-resistant starter strains based on the knowledge of resistance mechanisms developed by LAB and a better understanding of phage-host interactions (Sturino & Klaenhammer, 2006). Described mechanisms of phage resistance expand from blocking adsorption, restriction/ modification enzymes, to abortive infection systems that interfere with phage DNA replication, morphogenesis and release. Clustered regularly interspaced short palindromic repeats (CRISPRs) located in the genomes of host bacteria together with a group of associated proteins can also confer resistance to phages (Labrie et al., 2010). Recently, the response to phage infection in L. lactis has been approached by genome-wide transcriptomics (Fallico et al., 2011;Ainsworth et al., 2013). L. lactis appears to sense bacteriophage infection as a perturbation of its cell envelope and mounts a response targeted to the cell wall, activating regulators of the cell envelope stress response such as the two-component system CesSR.One of the members of the CesSR regulon in L. lactis is the ftsH gene (Martínez et al., 2007). ftsH encodes a conserved AAA (ATPase associated with various cellular activities)-type membrane protease involved in stress response and protein quality control (Ito & Akiyama, 2005;Narberhaus et al., 2009). In this work, we analysed the impact of the ftsH null mutation on the life cycle of the P335 temperate phage TP712, which is able to infect and lysogenize L. lactis MG1363 (Gasson, 1983) and derivatives thereof. The complete TP712 nt sequence has been determined (GenBank accession number AY766464) essentially as described by Wegmann et al. (2012).Preliminary experiments revealed that in standard plaque assays (Lillehaug, 1997), the efficiency of plaquing (EOP) of this phage on an available non-polar and in-frame L. lactis mutant lacking ftsH (Pinto et al., 2011) was reduced to 1.5610 25 when compared to its parent L. lactis NZ9000. Upon complementation with the plasmid pUK200 : : ftsH, ...

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“…In the simplest model, the proteases catalyze unfolding by pulling at the polypeptide chain, perhaps simply as a consequence of the translocation of the polypeptide chain into the degradation channel [1]. Once the protein reaches the proteolytic sites, it is hydrolysed into 3-30 amino acids-long peptides [7,8] (Figure 2). …”

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confidence: 99%

Protein targeting to ATP-dependent proteases

Inobe

Matouschek

2008

Current Opinion in Structural Biology

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ATP-dependent proteases control diverse cellular processes by degrading specific regulatory proteins. Understanding how these regulatory proteins are targeted to ATP-dependent proteases is of central importance to understanding their biological role as regulators. Recent work has shown that protein substrates are specifically transferred to ATP-dependent proteases through different routes. These routes can function in parallel or independently. In all of these targeting mechanisms it can be useful to separate two steps: substrate binding to the protease and initiation of degradation.To be active, newly synthesized protein chains must fold into three-dimensional structures, but regulated unfolding is also critically important in some biological processes, such as protein degradation by ATP-dependent proteases and protein translocation across membranes [1]. Unfolding is required during degradation because the proteolytic sites of the ATP-dependent proteases are sequestered deep inside the proteases' structures and accessible only through narrow openings. Similarly, unfolding is required during several translocation processes because the protein import channels in some organelles are not wide enough for native proteins to fit through them. The mechanisms of unfolding in both types of processes are similar to each other but different from that of unfolding induced by heat or chemical denaturants. Here we discuss how the requirement for protein unfolding during degradation affects the way ATPdependent proteases select their substrates. ATP-dependent proteasesATP-dependent proteases degrade short-lived regulatory proteins and thereby control cellular processes such as signal transduction, cell cycle, and gene transcription. The proteases also clear misfolded and aggregated proteins from the cell and produce some of the peptides to be displayed at cell surface as part of adaptive immune response. In eukaryotes, these functions are performed mainly by the proteasome. In prokaryotes and the organelles of eukaryotes, the functions are fulfill by analogues of the proteasome, such as the ClpAP, ClpXP, HslUV, FtsH, and Lon proteases. Although ATP-dependent proteases show only relatively little sequence identity, they share a common architecture [2].The ATP-dependent proteases all form large multisubunit particles (Figure 1). In the simplest case, FtsH protease, the particle consists 6 copies of a 71 kDa subunit forming a complex of approximately 425 kDa, and in the most complex case, the proteasome, the particle consists of some 40 different subunits forming a complex of 2 MDa molecular weight [3,4]. The subunits are mostly arranged in six or seven subunit rings that stack on top of each other to

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Proteolysis of the phage λ CII regulatory protein by FtsH (HflB) of Escherichia coli

Cited by 133 publications

References 41 publications

Subunit Organization of a Synechocystis Hetero-Oligomeric Thylakoid FtsH Complex Involved in Photosystem II Repair

Subunit Organization of a Synechocystis Hetero-Oligomeric Thylakoid FtsH Complex Involved in Photosystem II Repair

Lack of the host membrane protease FtsH hinders release of the Lactococcus lactis bacteriophage TP712

Protein targeting to ATP-dependent proteases

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