Literature DB >> 1648513

Autoprocessing of Drosophila copia gag precursor to generate a unique laminate structure in Escherichia coli.

K Yoshioka1, H Kanda, S Kondo, S Togashi, T Miyake, T Shiba.   

Abstract

Drosophila copia protease is likely to be encoded in the gag gene. We have expressed copia gag polyprotein precursor in E. coli. The gag precursor was correctly processed to generate a unique laminate structure in E. coli. The processing was almost completely blocked by a mutation at the putative active site of copia protease, and resulted in accumulation of the precursor. Furthermore, the laminate structure was not found in E. coli expressing the mutant precursor. These results indicate that the protease is involved in cleaving the gag precursor itself. Also, the assembly of copia gag protein should correlate to the autoprocessing of copia gag polyprotein precursor.

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Year:  1991        PMID: 1648513     DOI: 10.1016/0014-5793(91)80718-i

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


  2 in total

1.  Structures formed by the recombinant derivate of the gypsy retrovirus structural protein Gag in bacterial cells.

Authors:  B V Syomin; N A Kazilo; O G Leonova; Yu L Ivanova; Y V Ilyin; V I Popenko
Journal:  Dokl Biochem Biophys       Date:  2007 Nov-Dec       Impact factor: 0.788

2.  Isolation and characterization of recombinant Drosophila Copia aspartic proteinase.

Authors:  Senarath B P Athauda; Katsuji Yoshioka; Tadayoshi Shiba; Kenji Takahashi
Journal:  Biochem J       Date:  2006-11-01       Impact factor: 3.857

  2 in total

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