The N-terminal domain of the replication initiator protein RepE is a dimerization domain forming a stable dimer

Nakamura, Akira; Kakemoto, Hirofumi; Kobayashi, Gengo; Kita, Akiko; Wada, Chieko; Miki, Kunio

doi:10.1016/j.bbrc.2004.01.018

Cited by 7 publications

(5 citation statements)

References 13 publications

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“…5(C)] fit the model of TrfA. As it was shown for RepA and RepE45 we predict that only one, the N‐terminal WH domain, is involved in dimerization, whereas both WH1 and WH2 domains of TrfA are involved in interactions with DNA. Consistent with this prediction, the deletion mutant TrfA(CΔ305) that lacks the predicted WH2 domain, forms a dimer structure but does not bind DNA.…”

Section: Resultssupporting

confidence: 60%

Conformation of a plasmid replication initiator protein affects its proteolysis by ClpXP system

Pierechod¹,

Nowak²,

Saari³

et al. 2009

Protein Science

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Proteins from the Rep family of DNA replication initiators exist mainly as dimers, but only monomers can initiate DNA replication by interaction with the replication origin (ori). In this study, we investigated both the activation (monomerization) and the degradation of the broad-host-range plasmid RK2 replication initiation protein TrfA, which we found to be a member of a class of DNA replication initiators containing winged helix (WH) domains. Our in vivo and in vitro experiments demonstrated that the ClpX-dependent activation of TrfA leading to replicationally active protein monomers and mutations affecting TrfA dimer formation, result in the inhibition of TrfA protein degradation by the ClpXP proteolytic system. These data revealed that the TrfA monomers and dimers are degraded at substantially different rates. Our data also show that the plasmid replication initiator activity and stability in E. coli cells are affected by ClpXP system only when the protein sustains dimeric form.

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Section: Resultssupporting

confidence: 60%

Conformation of a plasmid replication initiator protein affects its proteolysis by ClpXP system

Pierechod¹,

Nowak²,

Saari³

et al. 2009

Protein Science

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“…In mammals, the calpain activity is controlled in vivo by calpastatin, a peptide that is the only specific inhibitor of the calpain family discovered to date; its specificity is determined by the simultaneous binding of three calpastatin subdomains to both subunits of heterodimeric calpains [ 35 ]. Another line of investigation have shown that nitric oxide (NO)-donors such as S-nitroso-5-dimethylaminonaph-thalene-1-sulphonyl (dansyl-SNO), S-nitrosoglutathione (GSNO), (+/-)-(E)-4-ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide (NOR-3) and S-nitrosoacetylpenicillamine (SNAP) are able to block the enzyme activity of different classes of cysteine peptidases, including mammalian calpains, via NO-mediated S-nitrosylation of the cysteine catalytic residue [ 36 , 37 ].…”

Section: Calpains and Calpsmentioning

confidence: 99%

Calpains: Potential Targets for Alternative Chemotherapeutic Intervention Against Human Pathogenic Trypanosomatids

Branquinha

Marinho

Sangenito³

et al. 2013

CMC

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Abstract:The treatment for both leishmaniasis and trypanosomiasis, which are severe human infections caused by trypanosomatids belonging to Leishmania and Trypanosoma genera, respectively, is extremely limited because of concerns of toxicity and efficacy with the available anti-protozoan drugs, as well as the emergence of drug resistance. Consequently, the urgency for the discovery of new trypanosomatid targets and novel bioactive compounds is particularly necessary. In this context, the investigation of changes in parasite gene expression between drug resistant/sensitive strains and in the up-regulation of virulence-related genes in infective forms has brought to the fore the involvement of calpain-like proteins in several crucial pathophysiological processes performed by trypanosomatids. These studies were encouraged by the publication of the complete genome sequences of three human pathogenic trypanosomatids, Trypanosoma brucei, Trypanosoma cruzi and Leishmania major, which allowed in silico analyses that in turn directed the identification of numerous genes with interesting chemotherapeutic characteristics, including a large family of calpain-related proteins, in which to date 23 genes were assigned as calpains in T. brucei, 40 in T. cruzi and 33 in L. braziliensis. In the present review, we intend to add to these biochemical/biological reports the investigations performed upon the inhibitory capability of calpain inhibitors against human pathogenic trypanosomatids.

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“…1B), as expected from the crystallographic structure of the protein. The structural integrity of RepE is also demonstrated by its ability to form dimers (26). Pulldown experiments (Fig.…”

Section: Dnaj Binds To the N-terminal Domain Of Repe With A 1:1mentioning

confidence: 99%

Structural Insights into the Chaperone Activity of the 40-kDa Heat Shock Protein DnaJ

Cuéllar

Perales-Calvo

Muga

et al. 2013

Journal of Biological Chemistry

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Background: DnaJ is an Hsp40 molecular chaperone able to bind and remodel native substrates as RepE, the repressor/ activator of plasmid F replication. Results: We describe the structure of DnaJ bound to RepE and two mutants and the resulting protein conformational changes. Conclusion: DnaJ conformational plasticity allows binding of different substrates. Significance: We present the first structure of an Hsp40 chaperone bound to a client.

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The N-terminal domain of the replication initiator protein RepE is a dimerization domain forming a stable dimer

Cited by 7 publications

References 13 publications

Conformation of a plasmid replication initiator protein affects its proteolysis by ClpXP system

Conformation of a plasmid replication initiator protein affects its proteolysis by ClpXP system

Calpains: Potential Targets for Alternative Chemotherapeutic Intervention Against Human Pathogenic Trypanosomatids

Structural Insights into the Chaperone Activity of the 40-kDa Heat Shock Protein DnaJ

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