Localization of Two Functions of the Phosphoribosyl Anthranilate Transferase of Escherichia Coli to Distinct Regions of the Polypeptide Chain

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1974 Feb 1

PMID 4590474

Citations 21

Authors

E N Jackson

C Yanofsky

Affiliations

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Abstract

The trpD gene specifies a polypeptide which has both glutamine amidotransferase and phosphoribosyl anthranilate (PRA) transferase activities. Deletions fusing segments of trpD to the gene preceding it in the operon, trpE, were selected in strains carrying various trpD point mutations. The selection procedure required both that a deletion enter trpE and that it restore the PRA transferase activity which the parent trpD point mutant lacked. Deletion mutants were found which had PRA transferase activity although the first third of trpD was deleted. The existence of the mutants proves that a terminal segment of trpD is sufficient to specify a polypeptide having PRA transferase activity. The location of the deletion end points on the genetic map of trpD defines the extent of the trpD segment required for PRA transferase activity. This segment did not overlap the initial region of trpD required to specify the glutamine amidotransferase function of the trpD polypeptide. These results support the hypothesis (M. Grieshaber and R. Bauerle, 1972; H. Zalkin and L. H. Hwang, 1971) that the bifunctional trpD polypeptide might have evolved by fusion of a gene specifying a glutamine amidotransferase with a gene directing PRA transferase synthesis.

Citing Articles

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References

Sarabhai A, Brenner S . A mutant which reinitiates the polypeptide chain after chain termination. J Mol Biol. 1967; 27(1):145-62. DOI: 10.1016/0022-2836(67)90357-9. View

Vogel H, Bonner D . Acetylornithinase of Escherichia coli: partial purification and some properties. J Biol Chem. 1956; 218(1):97-106. View

Margolin P, BAUERLE R . Determinants for regulation and initiation of expression of tryptophan genes. Cold Spring Harb Symp Quant Biol. 1966; 31:311-20. DOI: 10.1101/sqb.1966.031.01.041. View

ZALKIN H, Kling D . Anthranilate synthetase. Purification and properties of component I from Salmonella typhimurium. Biochemistry. 1968; 7(10):3566-73. DOI: 10.1021/bi00850a034. View

Ito J, Cox E, Yanofsky C . Anthranilate synthetase, an enzyme specified by the tryptophan operon of Escherichia coli: purification and characterization of component I. J Bacteriol. 1969; 97(2):725-33. PMC: 249752. DOI: 10.1128/jb.97.2.725-733.1969. View

Ito J, Yanofsky C . Anthranilate synthetase, an enzyme specified by the tryptophan operon of Escherichia coli: Comparative studies on the complex and the subunits. J Bacteriol. 1969; 97(2):734-42. PMC: 249753. DOI: 10.1128/jb.97.2.734-742.1969. View

Shapiro J, Adhya S . The galactose operon of E. coli K-12. II. A deletion analysis of operon structure and polarity. Genetics. 1969; 62(2):249-64. PMC: 1212271. DOI: 10.1093/genetics/62.2.249. View

Spudich J, Horn V, Yanofsky C . On the production of deletions in the chromosome of Escherichia coli. J Mol Biol. 1970; 53(1):49-67. DOI: 10.1016/0022-2836(70)90045-8. View

Queener S, GUNSALUS I . Anthranilate synthase enzyme system and complementation in Pseudomonas species. Proc Natl Acad Sci U S A. 1970; 67(3):1225-32. PMC: 283341. DOI: 10.1073/pnas.67.3.1225. View

10.

Nagano H, ZALKIN H, Henderson E . The anthranilate synthetase-anthranilate-5-phosphorribosylpyrophosphate phosphoribosyltransferase aggregate. On the reaction mechanism of anthranilate synthetase from Salmonella typhimurium. J Biol Chem. 1970; 245(15):3810-20. View

11.

Hwang L, ZALKIN H . Multiple forms of anthranilate synthetase-anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase from Salmonella typhimurium. J Biol Chem. 1971; 246(8):2338-45. View

12.

Yanofsky C, Horn V, Bonner M, Stasiowski S . Polarity and enzyme functions in mutants of the first three genes of the tryptophan operon of Escherichia coli. Genetics. 1971; 69(4):409-33. PMC: 1224543. DOI: 10.1093/genetics/69.4.409. View

13.

KANE J, Holmes W, Jensen R . Metabolic interlock. The dual function of a folate pathway gene as an extra-operonic gene of tryptophan biosynthesis. J Biol Chem. 1972; 247(5):1587-96. View

14.

Kuhn J, Pabst M, SOMERVILLE R . Mutant strains of Escherichia coli K-12 exhibiting enhanced sensitivity to 5-methyltryptophan. J Bacteriol. 1972; 112(1):93-101. PMC: 251384. DOI: 10.1128/jb.112.1.93-101.1972. View

15.

La Scolea Jr L, Balbinder E . Restoration of phosphoribosyl transferase activity by partially deleting the trpB gene in the tryptophan operon of Salmonella typhimurium. J Bacteriol. 1972; 112(2):877-85. PMC: 251499. DOI: 10.1128/jb.112.2.877-885.1972. View

16.

Jackson E, Yanofsky C . Internal deletions in the tryptophan operon of Escherichia coli. J Mol Biol. 1972; 71(2):149-61. DOI: 10.1016/0022-2836(72)90343-9. View

17.

Gibson F, Pittard J, Reich E . Ammonium ions as the source of nitrogen for tryptophan biosynthesis in whole cells of Escherichia coli. Biochim Biophys Acta. 1967; 136(3):573-6. DOI: 10.1016/0304-4165(67)90020-7. View