Sequential recognition of two distinct sites in  S by the proteolytic targeting factor RssB and ClpX

Stüdemann, Andrea; Noirclerc‐Savoye, Marjolaine; Klauck, Eberhard; Becker, Gisela; Schneider, Dominique; Hengge, Regine

doi:10.1093/emboj/cdg411

Cited by 94 publications

(83 citation statements)

References 42 publications

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“…The activity of MecA is modulated by the antiadaptor protein ComS, which binds with a higher affinity to MecA, subsequently releasing ComK, and activates competence development (37). The phosphorylated adaptor protein RssB targets RpoS in E. coli, the master regulator of the general stress response, for degradation by ClpXP (35,41). Thus, the phosphostate of RssB, which depends on the activity of the sensor kinase ArcB, is essential for its adaptor function (28).…”

Section: Discussionmentioning

confidence: 99%

Activity Control of the ClpC Adaptor McsB in Bacillus subtilis

et al. 2011

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Controlled protein degradation is an important cellular reaction for the fast and efficient adaptation of bacteria to ever-changing environmental conditions. In the low-GC, Gram-positive model organism Bacillus subtilis, the AAA؉ protein ClpC requires specific adaptor proteins not only for substrate recognition but also for chaperone activity. The McsB adaptor is activated particularly during heat stress, allowing the controlled degradation of the CtsR repressor by the ClpCP protease. Here we report how the McsB adaptor becomes activated by autophosphorylation on specific arginine residues during heat stress. In nonstressed cells McsB activity is inhibited by ClpC as well as YwlE.

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Section: Discussionmentioning

confidence: 99%

Activity Control of the ClpC Adaptor McsB in Bacillus subtilis

et al. 2011

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“…Another possible mechanism is that NblA tags PBS for the cellular proteolytic machinery, in analogy to e.g. ubiquitin that covalently binds to other proteins and makes them accessible to the 26 S proteasome or like the response regulator RssB that triggers the ClpXP-dependent degradation of the S subunit of RNA polymerase in E. coli (38,39). If NblA functions by marking phycobilisomes in such a manner, a protease should be found that is able to degrade phycobiliproteins.…”

Section: Discussionmentioning

confidence: 99%

Crystal Structure of NblA from Anabaena sp. PCC 7120, a Small Protein Playing a Key Role in Phycobilisome Degradation

Bienert

Baier²,

Volkmer³

et al. 2006

Journal of Biological Chemistry

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Cyanobacterial light-harvesting complexes, the phycobilisomes, are proteolytically degraded when the organisms are starved for combined nitrogen, a process referred to as chlorosis or bleaching. Gene nblA, present in all phycobilisome-containing organisms, encodes a protein of about 7 kDa that plays a key role in phycobilisome degradation. The mode of action of NblA in this degradation process is poorly understood. Here we presented the 1.8-Å crystal structure of NblA from Anabaena sp. PCC 7120. In the crystal, NblA is present as a four-helix bundle formed by dimers, the basic structural units. By using pull-down assays with immobilized NblA and peptide scanning, we showed that NblA specifically binds to the ␣-subunits of phycocyanin and phycoerythrocyanin, the main building blocks of the phycobilisome rod structure. By site-directed mutagenesis, we identified amino acid residues in NblA that are involved in phycobilisome binding. The results provided evidence that NblA is directly involved in phycobilisome degradation, and the results allowed us to present a model that gives insight into the interaction of this small protein with the phycobilisomes.Cyanobacteria are photosynthetic prokaryotes, which perform planttype oxygenic photosynthesis. Light harvesting in these organisms is mainly mediated by phycobilisomes, large water-soluble multiprotein complexes that are attached to the cytoplasmic surface of the photosynthetic membrane. Phycobilisomes are composed of brilliantly colored phycobiliproteins, to which open chain tetrapyrrole chromophores are covalently attached, and of linker proteins, which, with one

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“…The parent fusion carries the full-length leader and 477 nt of the rpoS-coding region, deleting the region necessary for RpoS degradation (24). Thus, levels of RpoS-lac should reflect changes only in mRNA stability and translation.…”

Section: Rpos Stabilization In the Acee Mutant Is Dependent Upon Indumentioning

confidence: 99%

Stress sigma factor RpoS degradation and translation are sensitive to the state of central metabolism

Battesti

Majdalani

Gottesman

2015

Proc. Natl. Acad. Sci. U.S.A.

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RpoS, the stationary phase/stress sigma factor of Escherichia coli, regulates a large cohort of genes important for the cell to deal with suboptimal conditions. Its level increases quickly in the cell in response to many stresses and returns to low levels when growth resumes. Increased RpoS results from increased translation and decreased RpoS degradation. Translation is positively regulated by small RNAs (sRNAs). Protein stability is positively regulated by anti-adaptors, which prevent the RssB adaptor-mediated degradation of RpoS by the ClpXP protease. Inactivation of aceE, a subunit of pyruvate dehydrogenase (PDH), was found to increase levels of RpoS by affecting both translation and protein degradation. The stabilization of RpoS in aceE mutants is dependent on increased transcription and translation of IraP and IraD, two known antiadaptors. The aceE mutation also leads to a significant increase in rpoS translation. The sRNAs known to positively regulate RpoS are not responsible for the increased translation; sequences around the start codon are sufficient for the induction of translation. PDH synthesizes acetyl-CoA; acetate supplementation allows the cell to synthesize acetyl-CoA by an alternative, less favored pathway, in part dependent upon RpoS. Acetate addition suppressed the effects of the aceE mutant on induction of the antiadaptors, RpoS stabilization, and rpoS translation. Thus, the bacterial cell responds to lowered levels of acetyl-CoA by inducing RpoS, allowing reprogramming of E. coli metabolism.RssB | ClpXP | acetyl CoA | RpoS | pyruvate dehydrogenase

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Sequential recognition of two distinct sites in S by the proteolytic targeting factor RssB and ClpX

Cited by 94 publications

References 42 publications

Activity Control of the ClpC Adaptor McsB in Bacillus subtilis

Activity Control of the ClpC Adaptor McsB in Bacillus subtilis

Crystal Structure of NblA from Anabaena sp. PCC 7120, a Small Protein Playing a Key Role in Phycobilisome Degradation

Stress sigma factor RpoS degradation and translation are sensitive to the state of central metabolism

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