Enzymes of the Tryptophan Pathway in Three
            <i>Bacillus</i>
            Species

Hoch, Sallie O.; Crawford, Irving P.

doi:10.1128/jb.116.2.685-693.1973

Cited by 28 publications

(17 citation statements)

References 28 publications

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“…This behavior is reminiscent of the AS of various pseudomonad bacteria (36) and various members of the genus Bacillus (18,27). A further characterization of the Proteus AS will be presented in a subsequent publication (M. Lar-gen and W. L. Belser, manuscript in preparation).…”

Section: Resultsmentioning

confidence: 90%

Tryptophan biosynthetic pathway in the Enterobacteriaceae: some physical properties of the enzymes

Largen¹,

Belser²

1975

J Bacteriol

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Several physical properties of the first four enzymatic activities of the tryptophan pathway were examined using gel filtration and ion exchange chromatography. Five different patterns were noted. Differences in the anthranilate synthetase (AS) and phosphoribosylanthranilate transferase (PRT) defined these patterns. In all the organisms studied phosphoribosylanthranilate isomerase and indoleglycerol phosphate synthetase co-eluted from both diethylaminoethyl-cellulose and G-200 and thus probably are contained in a single polypeptide of 50,000 daltons. An AS-PRT complex was found in Citrobacter species, Enterobacter cloacae, and Erwinia dissolvens. In all the other bacteria examined AS and PRT were separate molecules. In Serratia marcescens, S. marinorubra, and Enterobacter liquefaciens, AS was 140,000 daltons and PRT was 45,000 daltons. In Erwinia carotavora and Enterobacter hafniae the AS was the same size as the Serratia species but the PRT was larger at 67,000 daltons. Two Proteus species had an AS and PRT of the same size as E. carotavora and E. hafniae but the Proteus AS was different in that it partially dissociated upon gel filtration. Aeramonas formicans was unique in its possession of an AS with a molecular weight of 220,000. The PRT of A. formicans was found to elute at 67,000 daltons. Possible paths of evolution of the tryptophan enzymes are discussed in terms of the reults of this study. The results presented here are also considered with respect to existing taxonomic schemes of the enteric bacteria. ucts of these genes, five different distribution patterns were found. These results were considered with respect to existing phylogenetic schemes and were used to clarify some of the natural relationships among the fungi. 239 on July 31, 2020 by guest

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Section: Resultsmentioning

confidence: 90%

Tryptophan biosynthetic pathway in the Enterobacteriaceae: some physical properties of the enzymes

Largen¹,

Belser²

1975

J Bacteriol

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“…Tryptophan-requiring strains were grown in the same medium, with an additional 20 pg of tryptophan per ml (which causes repression of the chromosomal trp genes) or 0.5 to 1 pg of tryptophan per ml (which results in derepression of the chromosomal trp genes [131). Cells were harvested by centrifugation, the pellets were suspended in the appropriate 0.8 M sucrose buffer or 40c% glycerol buffer (13), and cell-free extracts were prepared as previously described (13,14).…”

Section: Methodsmentioning

confidence: 99%

“…Enzyme assays were performed as previously described (13,14). Specific activities are reported in nanomoles of substrate disappearing or product forming per minute per milligram of protein.…”

Section: Methodsmentioning

confidence: 99%

Insertional Inactivation of trpC in Cloned Bacillus trp Segments: Evidence for a Polar Effect on trpF

et al. 1979

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Plasmid pUB110 was previously used as a vector to clone fragments of deoxyribonucleic acid that complement the trpC2 mutation in Bacillus subtilis from endonuclease EcoRI digested B. licheniformis, B. pumilus, and B. subtilis cellular deoxyribonucleic acid. Each of several such trp plasmids was subsequently shown to contain a segment of the trp gene cluster on the basis of genetic complementing activity. In the present study, analysis of the Trp enzyme levels in B. subtilis harboring the constructed trp plasmids confirms the genetic constitution of the plasmids. Thus, plasmids that complement mutations in specific trp genes specify the corresponding enzyme activities. The levels of the plasmid-specified Trp enzymes in B. subtilis were generally above the repressed level of the chromosomally specified Trp enzymes and equal to or below the derepressed levels of the chromosomally specified.Trp enzymes. Certain cloned trp segments contain a single HindIlI-sensitive site. Insertion of HindIll-generated deoxyribonucleic acid fragments into these trp plasmids resulted in inactivation of trpC complementing activity, loss of the trpC-specified enzyme activity, and a 10-fold reduction in the specific activity of the plasmid-specified trpF product. The HindIII insertions had no detectable effect on the level of the trpD product, nor did the insertions detectably alter plasmid-specified complementing activity other than to abolish trpC complementation. Removal of the HindIII insertions was accompanied by recovery of trpC complementing activity and restoration of the trpCand trpF-determined enzymes to the levels specified by the parent plasmids.

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“…pUBl1O was used to clone a "trpF-complementing" EcoRI-generated fragment of the chromosome DNA isolated from BpB503, a tipC mutant of B. pumilus NRRL B-3275 (9). The initial transformation recipient for cloning was T12, a trpF point mutant of B. subtilis ( Table 1).…”

Section: 000}mentioning

confidence: 99%

Recombination between compatible plasmids containing homologous segments requires the Bacillus subtilis recE gene product

Keggins¹,

Duvall²,

Lovett³

1978

J Bacteriol

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Plasmid pSL103 was previously constructed by cloning a Trp fragment (-2.3 x 106 daltons) from restriction endonuclease EcoRI-digested chromosome DNA of Bacillus pumilus using the neomycin-resistance plasmid pUBi10 (-2.8 x 106 daltons) as vector and B. subtilis as transformation recipient. In the present study the EcoRI Trp fragment from pSL103 was transferred in vitro to EcoRI fragments of the Bacillus plasmid pPL576 to determine the ability of the plasmid fragments to replicate in B. subtilis. Endonuclease EcoRI digestion of pPL576 (-28 x 106 daltons) generated three fragments having molecular weights of about 13 x 106 (the A fragment), 9.5 x 106 (B fragment), and 6.5 x 106 (C fragment). Trp derivatives of pPL576 fragments capable of autonomous replication in B. subtilis contained the B fragment (e.g., pSL107) or both the B and C fragments (e.g., pSL108). Accordingly, the B fragment of pPL576 contains information essential for autonomous replication. pSL107 and pSL108 are compatible with pUBilO. Constructed derivatives of the compatible plasmids pPL576 and pUBllO, harboring genetically distinguishable EcoRI-generated Trp fragments cloned from the DNA of a B. pumilus strain, exhibited relatively high-frequency recombination for a trpC marker when the plasmid pairs were present in a recombinationproficient strain of B. subtilis. No recombination was detected when the host carried the chromosome mutation recE4. Therefore, the recE4 mutation suppresses recombination between compatible plasmids that contain homologous segments.

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Enzymes of the Tryptophan Pathway in Three Bacillus Species

Cited by 28 publications

References 28 publications

Tryptophan biosynthetic pathway in the Enterobacteriaceae: some physical properties of the enzymes

Tryptophan biosynthetic pathway in the Enterobacteriaceae: some physical properties of the enzymes

Insertional Inactivation of trpC in Cloned Bacillus trp Segments: Evidence for a Polar Effect on trpF

Recombination between compatible plasmids containing homologous segments requires the Bacillus subtilis recE gene product

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