Genetic organization and nucleotide sequence of the stability locus of IncFII plasmid NR1

Tabuchi, Akira; Min, You-Nong; Kim, Choon Kwang; Fan, Yanting; Womble, David D.; Rownd, Robert H.

doi:10.1016/0022-2836(88)90282-3

Cited by 38 publications

(72 citation statements)

References 51 publications

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“…Little is known about the function of the third bacterial protein with a significant pattern match. The E. coli protein StbA appears to be involved in plasmid stabilityi.e., deletion mutants suffer from unstable inheritance of certain low copy number plasmids (28). In the family described here, StbA is unusual in that it appears to lack subdomain IIb (Figs.…”

Section: Resultsmentioning

confidence: 80%

An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins.

Bork

Sander

Valencia

1992

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

764

633

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An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp7O heat shock proteins (structural ABSTRACTThe functionally diverse actin, hexokinase, and hsp7O protein families have in common an ATPase domain of known three-dimensional structure. Optimal superposition of the three structures and alignment ofmany sequences in each of the three families has revealed a set of common conserved residues, distributed in five sequence motifs, which are involved in ATP binding and in a putative interdomain hinge. From the multiple sequence aliment in these motifs a pattern of amino acid properties required at each position is defined. The discriminatory power of the pattern is in part due to the use of several known three-dimensional structures and many sequences and in part to the "property" method ofgeneralizing from observed amino acid frequencies to amino acid fitness at each sequence position. A sequence data base search with the pattern significantly matches sugar kinases, such as fuco-, glucono-, xylulo-, ribulo-, and glycerokinase, as well as the prokaryotic cell cycle proteins MreB, FtsA, and StbA. These are predicted to have subdomains with the same tertiary structure as the ATPase subdomains Ia and Ha of hexokinase, actin, and Hsc7O, a very similar ATP binding pocket, and the capacity for interdomain hinge motion accompanying functional state changes. A common evolutionary origin for all of the proteins in this class is proposed.

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Section: Resultsmentioning

confidence: 80%

An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins.

Bork

Sander

Valencia

1992

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

764

633

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“…A low-copy-number stb+ plasmid introduced into the same cell with the PA.acZ fusion plasmid repressed (-galactosidase activity about 5-fold, whereas a high-copy-number stb+ plasmid repressed 13-galactosidase about 15-fold. IncFII plasmid NR1, like most low-copy-number plasmids that have been examined (1, 4, 23), encodes functions that ensure its stable inheritance in the population of cells (17,27). The stb (stability) locus of NR1 (17, 27), which may be equivalent to the parA locus of closely related IncFII plasmid Ri (11), is thought to participate in the partitioning of plasmid molecules to daughter cells during cell division, which is essential for stable plasmid inheritance.…”

mentioning

confidence: 99%

“…These genes encode trans-acting stability proteins of 36,000 and 13,000 Da, respectively (27), and are transcribed together from promoter PAB (19). The cis-acting DNA site is located at or near PAB and can stabilize a plasmid if StbA and StbB are provided in trans (20,27). Therefore, the stb locus of NR1 is basically similar to the stabilizing loci of plasmids F (sop) and P1 prophage (par), which also are composed of two genes that encode essential trans-acting proteins and a cis-acting site (1-3, 6, 12, 15, 21, 22, 24).…”

mentioning

confidence: 99%

“…Mutants BglII fragment that contains stbB and the 3' half of stbA ( Fig. 1) produce an overabundance of truncated StbA protein (11,27) and have a high rate of transcription of the remaining stb sequences (19). Other mutants that have a transposon insertion in stbA, which prevents transcription of the region downstream from the insertion including stbB, produce an overabundance of mRNA that hybridizes to probes from the upstream region of the operon (19).…”

mentioning

confidence: 99%

“…IncFII plasmid NR1, like most low-copy-number plasmids that have been examined (1,4,23), encodes functions that ensure its stable inheritance in the population of cells (17,27). The stb (stability) locus of NR1 (17,27), which may be equivalent to the parA locus of closely related IncFII plasmid Ri (11), is thought to participate in the partitioning of plasmid molecules to daughter cells during cell division, which is essential for stable plasmid inheritance.…”

mentioning

confidence: 99%

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Autoregulation of the stability operon of IncFII plasmid NR1

et al. 1992

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The stb locus of IncFII plasmid NR1, which mediates stable inheritance of the plasmid, is composed of an essential cis-acting DNA site located upstream from two tandem genes that encode essential stability proteins. The two tandem genes, stbA and stbB, are transcribed as an operon from promoter PAB. Using PAB-lacZ gene fusions, it was found that the stb operon is autoregulated. A low-copy-number stb+ plasmid introduced into the same cell with the PA.acZ fusion plasmid repressed (-galactosidase activity about 5-fold, whereas a high-copy-number stb+ plasmid repressed 13-galactosidase about 15-fold. IncFII plasmid NR1, like most low-copy-number plasmids that have been examined (1, 4, 23), encodes functions that ensure its stable inheritance in the population of cells (17,27). The stb (stability) locus of NR1 (17, 27), which may be equivalent to the parA locus of closely related IncFII plasmid Ri (11), is thought to participate in the partitioning of plasmid molecules to daughter cells during cell division, which is essential for stable plasmid inheritance. Mutations that inactivate the stb function result in plasmid instability, so that plasmid-free cells are segregated at a rate consistent with random distribution of plasmid copies at cell division (17,25).Within the 95-kb genome of the self-transmissible antibiotic resistance plasmid NR1 (30), stb is located approximately at coordinates 24.5 to 26.1 kb and is contained within a 1.7-kb region bounded by NaeI and TaqI restriction sites ( Fig. 1) (27). The three essential elements of the stb locus are a cis-acting DNA site and two tandem genes, stbA and stbB. These genes encode trans-acting stability proteins of 36,000 and 13,000 Da, respectively (27), and are transcribed together from promoter PAB (19). The cis-acting DNA site is located at or near PAB and can stabilize a plasmid if StbA and StbB are provided in trans (20,27). Therefore, the stb locus of NR1 is basically similar to the stabilizing loci of plasmids F (sop) and P1 prophage (par), which also are composed of two genes that encode essential trans-acting proteins and a cis-acting site (1-3, 6, 12, 15, 21, 22, 24). A primary difference among these plasmid-stabilizing loci is that for F and P1, the cis-acting partition sites lie downstream from the two genes, whereas for the stb locus of NR1, the site is upstream from the genes and may overlap promoter PAB. This fundamental difference may signal differences in the ways the loci function and in how they are regulated.Several lines of indirect evidence suggest that the stb operon is autoregulated. Mutants BglII fragment that contains stbB and the 3' half of stbA ( Fig. 1) produce an overabundance of truncated StbA protein (11,27) and have a high rate of transcription of the remaining stb sequences (19). Other mutants that have a transposon insertion in stbA, which prevents transcription of the region downstream from the insertion including stbB, produce an overabundance of mRNA that hybridizes to probes from the upstream region of the operon (19). Also, a...

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Partitioning of plasmid R1. The ParM protein exhibits ATPase activity and interacts with the centromere-like ParR-parC complex

Jensen¹,

Gerdes²

1997

Journal of Molecular Biology

112

108

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Genetic organization and nucleotide sequence of the stability locus of IncFII plasmid NR1

Cited by 38 publications

References 51 publications

An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins.

An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins.

Autoregulation of the stability operon of IncFII plasmid NR1

Partitioning of plasmid R1. The ParM protein exhibits ATPase activity and interacts with the centromere-like ParR-parC complex

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