Interaction between F Plasmid Partition Proteins SopA and SopB

Kim, Sook-Kyung; Shim, Jay

doi:10.1006/bbrc.1999.1317

Cited by 17 publications

(13 citation statements)

References 22 publications

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“…This localization of the domain that interacts with ParA is different from that in well-characterized plasmid systems. For example, in P1 (51) and F (27), the N terminus of ParB/SopB is essential for the interaction with ParA, and in the RP4/RK2 system, the central segment of KorB is essential (34). Recent data on ParB of C. crescentus localized the domain of interaction with ParA to the N-terminal 40 aa (9).…”

Section: Discussionmentioning

confidence: 99%

“…In the well-characterized plasmid partitioning systems, two components, ParA and ParB, are predicted to interact directly either at the centromere-like site (5,24) or at the autoregulated promoter of the parAB operon (ParB potentiates repression exerted by ParA) (10,39). Direct protein-protein interactions have been demonstrated so far for ParA and ParB of P1 (5,51), SopA and SopB of F (16,27), ParM and ParR of R1 (24), and IncC and KorB of RK2 (34,46). Recent studies of spo0J mutants of B. subtilis (2) and parAB mutants of C. crescentus (9) also demonstrated the possibility of such interactions between chromosomal homologues.…”

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confidence: 97%

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ParB ofPseudomonas aeruginosa: Interactions with Its Partner ParA and Its TargetparSand Specific Effects on Bacterial Growth

et al. 2004

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 97%

ParB ofPseudomonas aeruginosa: Interactions with Its Partner ParA and Its TargetparSand Specific Effects on Bacterial Growth

et al. 2004

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“…The IncC protein was predicted to be involved in partition on the basis of sequence similarity to regions of the ParA and SopA partition proteins of plasmids P1 and F, respectively (62). Both the ParA and SopA proteins have been shown to interact with the cognate DNA-binding proteins ParB and SopB (10,15,18,38,47,61,95). The ParM protein of plasmid R1, which has no sequence relationship with ParA or SopA, but is thought to have a similar function in partition, interacts with the DNA-binding protein ParR (44 The discovery that KorB functions both as an active partition protein with IncC and a global transcriptional repressor is a remarkable finding that distinguishes the RK2 system from any other plasmid partition system.…”

Section: Discussionmentioning

confidence: 99%

“…Current models for active partition hold that the ATP-hydrolyzing protein and the DNA-binding protein interact to facilitate the formation of plasmid pairs or the positioning of the plasmids in the cell. There is good evidence for the interactions of these proteins in the P1, F, and R1 plasmid systems (10,18,38,44,47,95). If IncC and KorB have similar functions in partition, they may be expected to interact.…”

Section: ͼ10mentioning

confidence: 99%

Incompatibility Protein IncC and Global Regulator KorB Interact in Active Partition of Promiscuous Plasmid RK2

et al. 2000

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Replication of the broad-host-range, IncP␣ plasmid RK2 requires two plasmid loci: trfA, the replication initiator gene, and oriV, the origin of replication. While these determinants are sufficient for replication in a wide variety of bacteria, they do not confer the stable maintenance of parental RK2 observed in its hosts. The product of the incC gene has been proposed to function in the stable maintenance of RK2 because of its relatedness to the ParA family of ATPases, some of which are known to be involved in the active partition of plasmid and chromosomal DNA. Here we show that IncC has the properties expected of a component of an active partition system. The smaller polypeptide product of incC (IncC2) exhibits a strong, replicon-independent incompatibility phenotype with RK2. This incompatibility phenotype requires the global transcriptional repressor, KorB, and the target for incC-mediated incompatibility is a KorB-binding site (O B ). We found that KorB and IncC interact in vivo by using the yeast two-hybrid system and in vitro by using partially purified proteins. Elevated expression of the incC and korB genes individually has no obvious effect on Escherichia coli cell growth, but their simultaneous overexpression is toxic, indicating a possible interaction of IncC-KorB complexes with a vital host target. A region of RK2 bearing incC, korB, and multiple KorB-binding sites is able to stabilize an unstable, heterologous plasmid in an incC-dependent manner. Finally, elevated levels of IncC2 cause RK2 to aggregate, indicating a possible role for IncC in plasmid pairing. These findings demonstrate that IncC, KorB, and at least one KorB-binding site are components of an active partition system for the promiscuous plasmid RK2.

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“…This would identify the C terminus of Delta as the region of interaction with Omega. It has been shown previously (Kim & Shim, 1999;Ravin et al, 2003) that the C-terminal amino acids of F SopA protein are essential for its interaction with SopB.…”

Section: Delta and Omega Protein Interactionsmentioning

confidence: 99%

Mapping of the interactions between partition proteins Delta and Omega of plasmid pSM19035 from Streptococcus pyogenes

Dmowski

Jagura-Burdzy

2011

Microbiology

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Formation of the segrosome, a nucleoprotein complex crucial for proper functioning of plasmid partition systems, involves interactions between specific partition proteins (ParA-like and ParBlike), ATP and specific DNA sequences (the centromeric sites). Although partition systems have been studied for many years, details of the segrosome formation are not yet clear. Organization of the pSM19035-encoded partition system is unique; in contrast with other known par systems, here, the d and v genes do not constitute an operon. Moreover, Omega [a ParB-like protein which has a Ribbon-Helix-Helix (RHH) structure] recognizes multiple centromeric sequences located in the promoters of d, v and copS (copy-number control gene). The ParA-like protein Delta is a Walker-type ATPase. In this work, we identify the interaction domains and requirements for dimerization and hetero-interactions of the Delta and Omega proteins of pSM19035 plasmid. The RHH structures are involved in Omega dimerization in vivo and its N-terminal unstructured part is indispensable for association with Delta, both in vivo and in vitro. Omega does not need to form dimers to interact with Delta. ATP binding is not required for Delta dimerization but is important for interaction with Omega in vivo. The in vitro interaction between Delta and Omega depends on ATP but does not require the presence of specific DNA segments (the centromere) recognized by Omega. The C-terminal part of the Delta protein (aa 198-284) is indispensable for interaction with Omega. Delta most probably interacts with Omega as a dimer since two amino acid substitutions in a conserved region between the A9 and B motifs abolish both the dimerization of Delta and its interaction with Omega.

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Interaction between F Plasmid Partition Proteins SopA and SopB

Cited by 17 publications

References 22 publications

ParB ofPseudomonas aeruginosa: Interactions with Its Partner ParA and Its TargetparSand Specific Effects on Bacterial Growth

ParB ofPseudomonas aeruginosa: Interactions with Its Partner ParA and Its TargetparSand Specific Effects on Bacterial Growth

Incompatibility Protein IncC and Global Regulator KorB Interact in Active Partition of Promiscuous Plasmid RK2

Mapping of the interactions between partition proteins Delta and Omega of plasmid pSM19035 from Streptococcus pyogenes

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