Literature DB >> 2121534

The reaction specificities of the pea and a cyanobacterial thylakoid processing peptidase are similar but not identical.

T P Wallace1, C Robinson, C J Howe.   

Abstract

The thylakoid processing peptidase from the cyanobacterium Phormidium laminosum has been extracted from thylakoid membranes by solubilization with Triton X-100. Its reaction specificity has been compared with the analogous pea peptidase by processing in vitro of radiolabelled wheat and P. laminosum thylakoid lumenal precursor polypeptides. The cyanobacterial polypeptide is processed to the mature size through an intermediate by the P. laminosum peptidase, but to a polypeptide that has a slightly greater apparent molecular weight than the intermediate by the pea peptidase. Both peptidases correctly process the wheat polypeptide. This suggests that the reaction specificities of the two peptidases are similar, but not identical.

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Year:  1990        PMID: 2121534     DOI: 10.1016/0014-5793(90)80468-x

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  4 in total

Review 1.  Proteolysis in protein import and export: signal peptide processing in eu- and prokaryotes.

Authors:  M Müller
Journal:  Experientia       Date:  1992-02-15

2.  Keep the balloon deflated: the significance of protein maturation for thylakoid flattening.

Authors:  Joshua K Endow; Nicholas J Ruppel; Kentaro Inoue
Journal:  Plant Signal Behav       Date:  2010-06

3.  Cloning and sequence analysis of a signal peptidase I from the thermophilic cyanobacterium Phormidium laminosum.

Authors:  J C Packer; D André; C J Howe
Journal:  Plant Mol Biol       Date:  1995-01       Impact factor: 4.076

4.  Functional diversification of thylakoidal processing peptidases in Arabidopsis thaliana.

Authors:  Shih-Chi Hsu; Joshua K Endow; Nicholas J Ruppel; Rebecca L Roston; Amy J Baldwin; Kentaro Inoue
Journal:  PLoS One       Date:  2011-11-07       Impact factor: 3.240

  4 in total

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