Literature DB >> 350289

Folate polyglutamates in T4D bacteriophage and T4D-infected Escherichia coli.

K Nakamura, L M Kozloff.   

Abstract

The folate compound which is a structural component of the Escherichia coli T-even bacteriophage baseplates, has been identified as the hexaglutamyl form of folic acid using a new chromatographic procedure (Baugh, C.M., Braverman, E. and Nair, M.G. (1974) Biochemistry 13, 4952-4957). It has also been found that the host cell contains a variety of polyglutamyl forms of folic acid. The major form is the triglutamate (about 50%) but small amounts of higher molecular weight folates including the octaglutamate (1.8%) have been identified. Upon infection with wild-type T4D bacteriophage there is a shift in the distribution of the folate compounds so that the folyl polyglutamyl compounds having the higher molecular weights are increased. Infection of E. coli with baseplate mutants of T4D containing an amber mutation in gene 28 resulted in the formation of significant amounts (over 7%) of folate compound(s) of molecular weight much higher than those observed either in uninfected cells or cells infected with wild-type T4D. It is suggested that the T4D gene 28 product functions to cleave glutamate residues from high molecular weight folyl polyglutamates to increase the availability of the folyl hexaglutamate for virus assembly.

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Year:  1978        PMID: 350289     DOI: 10.1016/0304-4165(78)90144-7

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  6 in total

1.  Analysis of T4 bacteriophage deletion mutants that lack td and frd genes.

Authors:  Y Wang; C K Mathews
Journal:  J Virol       Date:  1989-11       Impact factor: 5.103

2.  Dual functions of bacteriophage T4D gene 28 product: structural component of the viral tail baseplate central plug and cleavage enzyme for folyl polyglutamates. I. Identification of T4D gene 28 product in the tail plug.

Authors:  L M Kozloff; J Zorzopulos
Journal:  J Virol       Date:  1981-12       Impact factor: 5.103

3.  Structural role of the polyglutamate portion of the folate found in T4D bacteriophage baseplate.

Authors:  L M Kozloff; L K Crosby; C M Baugh
Journal:  J Virol       Date:  1979-11       Impact factor: 5.103

4.  Bacteriophage T4-coded dihydrofolate reductase: synthesis, turnover, and location of the virion protein.

Authors:  R A Mosher; C K Mathews
Journal:  J Virol       Date:  1979-07       Impact factor: 5.103

5.  Dual functions of bacteriophage T4D gene 28 product: structural component of the viral tail baseplate central plug and cleavage enzyme for folyl polyglutamates. II. Folate metabolism and polyglutamate cleavage activity of uninfected and infected Escherichia coli cells and bacteriophage.

Authors:  L M Kozloff; M Lute
Journal:  J Virol       Date:  1981-12       Impact factor: 5.103

Review 6.  Enzymatic synthesis and function of folylpolyglutamates.

Authors:  J J McGuire; J R Bertino
Journal:  Mol Cell Biochem       Date:  1981-08-11       Impact factor: 3.396

  6 in total

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