A Sporulation Gene in <i>Coxiella burnetii?</i>

Oswald, Winfried; Thiele, D.

doi:10.1111/j.1439-0450.1993.tb00151.x

Cited by 15 publications

(10 citation statements)

References 18 publications

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“…6 and 7 demonstrate that FtsK has blocks of very high sequence similarity to the SpoIIIE protein of B. subtilis (64) and to polypeptides of unknown function from C. burnetii (42) and C. jejuni (38). The closest similarity, especially in the N-terminal region, is with the C. burnetii SpoIIIE protein, which is in accord with the closer taxonomic relationship between these two species, but the similarity to each of them is very high.…”

Section: Discussionsupporting

confidence: 68%

A new Escherichia coli cell division gene, ftsK

1995

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A mutation in a newly discovered Escherichia coli cell division gene, ftsK, causes a temperature-sensitive late-stage block in division but does not affect chromosome replication or segregation. This defect is specifically suppressed by deletion of dacA, coding for the peptidoglycan DD-carboxypeptidase, PBP 5. FtsK is a large polypeptide (147 kDa) consisting of an N-terminal domain with several predicted membrane-spanning regions, a proline-glutamine-rich domain, and a C-terminal domain with a nucleotide-binding consensus sequence. FtsK has extensive sequence identity with a family of proteins from a wide variety of prokaryotes and plasmids. The plasmid proteins are required for intercellular DNA transfer, and one of the bacterial proteins (the SpoIIIE protein of Bacillus subtilis) has also been implicated in intracellular chromosomal DNA transfer.Cell division is a much-studied process in Escherichia coli, and a number of division genes and proteins are now well known (17). The cell division-specific proteins include FtsZ, which forms a ring around the inside of the cell membrane during division (9,11,16,39,40,45), and a set of membraneassociated proteins (the products of ftsL, -I, -W, -Q, -A, and possibly others) that include the septum-specific peptidoglycan transpeptidase and transglycosylase, PBP 3 (the ftsI gene product). The action of these proteins results in the formation of a covalently cross-linked double-layered septum across the cell center (43). Splitting of the bonds between the two completed layers (accompanied by invagination of the outer membrane) completes the process of cell division (3,63).A mutant, TOE44, described for the first time in this paper, was originally isolated in a search for conditional mutants that are blocked in cell division but in which the temperaturesensitive period is only a short fraction of the cell cycle (6). The same search produced the first mutations in ftsQ, as well as new ftsI and ftsA alleles (6). This set of mutants has now been rescreened to look for any that have a block at a late stage in division.Many mutations cause an indirect block to cell division because they elicit the SOS response (by interference with DNA replication) and thus induce the synthesis of the FtsZ inhibitor, SfiA (26). Mutations (e.g., in dnaK or groE) that elicit the heat shock response also cause a block in division that can be reversed by increased amounts of FtsZ in some cases (13). Mutants of these kinds appear to be blocked in a very early stage in division, the stage at which FtsZ acts. The remaining mutants in this collection have now been screened for those that are blocked later in division. The present investigation of TOE44 was prompted by the finding that, at 42ЊC, this mutant appears to be blocked at a very late stage. The mutation responsible has been mapped and shown to be in a previously unidentified gene, ftsK, adjacent to lrp, the gene for the leucine-responsive protein (55,(59)(60)(61)(62). We find that the mutant phenotype is specifically suppressed by the deletion o...

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Section: Discussionsupporting

confidence: 68%

A new Escherichia coli cell division gene, ftsK

1995

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“…As one way of elucidating the function of this domain, we searched for sequence similarities in protein sequence data bases. Strong sequence similarities were reported previously between SpoIIIE and chromosomal genes from diverse bacteria, Coxiella burnetii (Oswald and Thiele 1993) and Campylobacter jejtmi (Miller et al 1994). Unfortunately, the functions of these genes are not yet known.…”

Section: The Carboxy-terminal Domain Of Spoliie Resembles the Tra Prosupporting

confidence: 77%

A conjugation-like mechanism for prespore chromosome partitioning during sporulation in Bacillus subtilis.

Wu¹,

Lewis²,

et al. 1995

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“…Since this peptide is not a part of three highly conserved motifs characterizing class II synthetases (23), and is not present in four prokaryotic SerRS enzymes (5,7,6,24) (Fig. 1), a non-catalytic role was proposed.…”

Section: Resultsmentioning

confidence: 99%

“…The combination of biophysical, biochemical and genetic techniques have significantly deepened our understanding of the structure and function of these enzymes (1)(2)(3). The amino acid sequences of seryl-tRNA synthetases from Escherichia coli (4), Thermus thermophilus (5), Bacillus subtilis (6), Coxiella burnetii (7), Saccharomyces cerevisiae (8), Chinese hamster (partial) (9), and human 1 are known. According to common structural motifs they are typical representatives of class II synthetases (10).…”

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confidence: 99%

The C-terminal Extension of Yeast Seryl-tRNA Synthetase Affects Stability of the Enzyme and Its Substrate Affinity

Weygand-Đurašević

Lenhard

Filipić

et al. 1996

Journal of Biological Chemistry

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Saccharomyces cerevisiae seryl-tRNA synthetase (SerRS) contains a 20-amino acid C-terminal extension, which is not found in prokaryotic SerRS enzymes. A truncated yeast SES1 gene, lacking the 60 base pairs that encode this C-terminal domain, is able to complement a yeast SES1 null allele strain; thus, the C-terminal extension in SerRS is dispensable for the viability of the cell. However, the removal of the C-terminal peptide affects both stability of the enzyme and its affinity for the substrates. The truncation mutant binds tRNA with 3.6-fold higher affinity, while the K m for serine is 4-fold increased relative to the wild-type SerRS. This indicates the importance of the C-terminal extension in maintaining the overall structure of SerRS.Aminoacyl-tRNA synthetases are essential enzymes that catalyze the esterification of an amino acid to its cognate tRNA with exquisite specificity. The combination of biophysical, biochemical and genetic techniques have significantly deepened our understanding of the structure and function of these enzymes (1-3). The amino acid sequences of seryl-tRNA synthetases from Escherichia coli (4), Thermus thermophilus (5), Bacillus subtilis (6), Coxiella burnetii (7), Saccharomyces cerevisiae (8), Chinese hamster (partial) (9), and human 1 are known. According to common structural motifs they are typical representatives of class II synthetases (10). The crystal structures of two prokaryotic enzymes isolated from E. coli (11) and T. thermophilus (12) are quite similar, as is their mode of interaction with tRNA Ser . We have been working with yeast SerRS, 2 which shows only moderate similarity (about 30%) with prokaryotic seryl-tRNA synthetases on the level of the primary structure (5), but still recognizes bacterial tRNA Ser and can functionally substitute for the bacterial enzyme in vivo (13). The overexpression of the yeast SES1 gene in E. coli generated high amounts of functional enzyme (13), although with somewhat lower specific activity and slightly different electrophoretic mobility 3 compared to the enzyme isolated from yeast. This raises the possibility that the yeast enzyme may not be modified or folded correctly in the bacterial host. In this paper we describe the purification of yeast SerRS from an overproducing strain of S. cerevisiae. The alignment of the primary sequences of all SerRS proteins reveals that the enzymes from yeast (8), Chinese hamster (9), and human 1 contain C-terminal extension between 20 and 48 amino acids long not found in prokaryotic synthetases. We speculated whether this peptide was important for maintaining the structure of the eukaryotic enzymes or if it had another function. Thus, we deleted the part of the S. cerevisiae SES1 gene encoding the short C-terminal domain and analyzed the expressed truncated protein. (14). Selection for yeast auxotrophic markers was done in a medium of 0.67% nitrogen base and 2% glucose lacking amino acids, supplemented as needed with adenine (20 g/ml), uracil (20 g/ml), and amino acids (20 -30 g/ml). Sporulation mediu...

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A Sporulation Gene in Coxiella burnetii?

Cited by 15 publications

References 18 publications

A new Escherichia coli cell division gene, ftsK

A new Escherichia coli cell division gene, ftsK

A conjugation-like mechanism for prespore chromosome partitioning during sporulation in Bacillus subtilis.

The C-terminal Extension of Yeast Seryl-tRNA Synthetase Affects Stability of the Enzyme and Its Substrate Affinity

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