Secretion of alpha-amylase from Pseudoalteromonas haloplanktis TAB23: two different pathways in different hosts.
نویسندگان
چکیده
Secretion of cold-adapted alpha-amylase from Pseudoalteromonas haloplanktis TAB23 was studied in three Antarctic bacteria. We demonstrated that the enzyme is specifically secreted in the psychrophilic hosts even in the absence of a protein domain that has been previously reported to be necessary for alpha-amylase secretion in Escherichia coli. The occurrence of two different secretion pathways in different hosts is proposed.
منابع مشابه
A novel genetic system for recombinant protein secretion in the Antarctic Pseudoalteromonas haloplanktis TAC125
BACKGROUND The final aim of recombinant protein production is both to have a high specific production rate and a high product quality. It was already shown that using cold-adapted bacteria as host vectors, some "intractable" proteins can be efficiently produced at temperature as low as 4 degrees C. RESULTS A novel genetic system for the production and secretion of recombinant proteins in the ...
متن کاملDevelopment of an improved Pseudoalteromonas haloplanktis TAC125 strain for recombinant protein secretion at low temperature
BACKGROUND In a previous paper, we reported the accomplishment of a cold gene-expression system for the recombinant secretion of heterologous proteins in Pseudoalteromonas haloplanktis TAC125. This system makes use of the psychrophilic alpha-amylase from P. haloplanktis TAB23 as secretion carrier, and allows an effective extra-cellular addressing of recombinant proteins. However, Pseudoalteromo...
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A gene (amyA) encoding an extracellular alpha-amylase from a marine bacterium Pseudoalteromnonas sp. MY-1 was cloned and expressed in Escherichia coli. It comprised an open-reading-frame of 2,007 base pairs and encoded a protein of 669 amino acids with a predicted molecular weight of 73,770 daltons and a pI of 5.15. The entire amino acid sequence of amyA gene showed 86% similarity to the alpha-...
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Background We have already shown that using cold-adapted bacteria as host vectors, some "intractable" proteins can be efficiently produced at temperature as low as 4°C [1,2]. Furthermore, we set up a "cold" gene-expression system implemented for the secretion of recombinant proteins in the Antarctic Gram-negative bacterium Pseudoalteromonas haloplanktis TAC125 (PhTAC125). Such a system could ef...
متن کاملExpression of psychrophilic genes in mesophilic hosts: assessment of the folding state of a recombinant alpha-amylase.
Alpha-Amylase from the antarctic psychrophile Altermonas haloplanktis is synthesized at 0 +/- 2 degrees C by the wild strain. This heat-labile alpha-amylase folds correctly when overexpressed in Escherichia coli, providing the culture temperature is sufficiently low to avoid irreversible denaturation. In the described expression system, a compromise between enzyme stability and E. coli growth r...
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ورودعنوان ژورنال:
- Journal of bacteriology
دوره 184 20 شماره
صفحات -
تاریخ انتشار 2002