Abstract:
:Complex-formation between a truncated staphylococcal Protein A produced in Escherichia coli and a native E coli molecular chaperone, DnaK, can be used for the purification of DnaK by IgG-affinity chromatography. The half-time constant for in vitro formation of the Protein A-DnaK complex is about 14 min. Complex-formation in the presence of ATP is faster, but pre-incubation of DnaK with ATP decreases the final amount of the complex. A second complex with a slower migration on native PAGE is formed when the ratio of DnaK to Protein A is increased. A derivative of Protein A, ZZ, which essentially contains only two modified domains of Protein A, did not bind DnaK. After insertion of a tryptophan-rich peptide close to the C-terminus, the resulting protein, ZZT3, became able to bind DnaK. The binding of these three proteins to DnaK correlates with proteolysis in E coli, indicating a possible role for the binding of DnaK in the control of proteolysis.
journal_name
Biotechnol Appl Biochemjournal_title
Biotechnology and applied biochemistryauthors
Gustavsson K,Bergman T,Veide A,Enfors SOsubject
Has Abstractpub_date
1997-04-01 00:00:00pages
173-80issue
2eissn
0885-4513issn
1470-8744journal_volume
25pub_type
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journal_title:Biotechnology and applied biochemistry
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journal_title:Biotechnology and applied biochemistry
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journal_title:Biotechnology and applied biochemistry
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journal_title:Biotechnology and applied biochemistry
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更新日期:1993-06-01 00:00:00
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journal_title:Biotechnology and applied biochemistry
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doi:
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