Dataset Information

Trans-cyclization of phosphatidylinositol catalyzed by phospholipase C from Streptomyces antibioticus.

ABSTRACT: Calcium-dependent phosphatidylinositol-specific phospholipase C from Streptomyces antibioticus (saPLC1) catalyzes the cleavage of phosphatidylinositol (PI) by an unusual mechanism involving a 1,6-cyclization with formation of inositol trans-1,6-cyclic phosphate (1,6-IcP), rather then inositol cis-1,2-cyclic phosphate (1,2-IcP). This conclusion has been reached based on the comparison of the released cyclic phosphate intermediate by the H16A mutant of saPLC1 with a genuine 1,6-IcP synthesized by a chemoenzymatic approach.

SUBMITTER: Bai C

PROVIDER: S-EPMC2734487 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature

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Trans-cyclization of phosphatidylinositol catalyzed by phospholipase C from Streptomyces antibioticus.

Bai Chuan C Zhao Li L Rebecchi Mario M Tsai Ming-Daw MD Bruzik Karol S KS

Journal of the American Chemical Society 20090601 24

Calcium-dependent phosphatidylinositol-specific phospholipase C from Streptomyces antibioticus (saPLC1) catalyzes the cleavage of phosphatidylinositol (PI) by an unusual mechanism involving a 1,6-cyclization with formation of inositol trans-1,6-cyclic phosphate (1,6-IcP), rather then inositol cis-1,2-cyclic phosphate (1,2-IcP). This conclusion has been reached based on the comparison of the released cyclic phosphate intermediate by the H16A mutant of saPLC1 with a genuine 1,6-IcP synthesized by ...[more]

PMID: 19492832

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Project description:We have examined the expression of pnp encoding the 3'-5'-exoribonuclease, polynucleotide phosphorylase, in Streptomyces antibioticus. We show that the rpsO-pnp operon is transcribed from at least two promoters, the first producing a readthrough transcript that includes both pnp and the gene for ribosomal protein S15 (rpsO) and a second, Ppnp, located in the rpsO-pnp intergenic region. Unlike the situation in Escherichia coli, where observation of the readthrough transcript requires mutants lacking RNase III, we detect readthrough transcripts in wild-type S. antibioticus mycelia. The Ppnp transcriptional start point was mapped by primer extension and confirmed by RNA ligase-mediated reverse transcription-PCR, a technique which discriminates between 5' ends created by transcription initiation and those produced by posttranscriptional processing. Promoter probe analysis demonstrated the presence of a functional promoter in the intergenic region. The Ppnp sequence is similar to a group of promoters recognized by the extracytoplasmic function sigma factors, sigma-R and sigma-E. We note a number of other differences in rspO-pnp structure and function between S. antibioticus and E. coli. In E. coli, pnp autoregulation and cold shock adaptation are dependent upon RNase III cleavage of an rpsO-pnp intergenic hairpin. Computer modeling of the secondary structure of the S. antibioticus readthrough transcript predicts a stem-loop structure analogous to that in E. coli. However, our analysis suggests that while the readthrough transcript observed in S. antibioticus may be processed by an RNase III-like activity, transcripts originating from Ppnp are not. Furthermore, the S. antibioticus rpsO-pnp intergenic region contains two open reading frames. The larger of these, orfA, may be a pseudogene. The smaller open reading frame, orfX, also observed in Streptomyces coelicolor and Streptomyces avermitilis, may be translationally coupled to pnp and the gene downstream from pnp, a putative protease.

Dataset Information

Trans-cyclization of phosphatidylinositol catalyzed by phospholipase C from Streptomyces antibioticus.

Publications

Trans-cyclization of phosphatidylinositol catalyzed by phospholipase C from Streptomyces antibioticus.

Similar Datasets

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