Abstract:
:Random sequences of 120-130 amino acid residues were inserted into a surface loop region of Escherichia coli RNase HI. This library was screened and about 10% of the clones were found to retain RNase H activity. Subsequent random mutagenesis led to an increase in RNase H activity and solubility of the protein. The inserted regions were found not to contribute to the secondary structure of the mutant protein. The high frequency of insertion of flexible sequences and the increase in the protein's function by further mutagenesis simulate one of the events in protein evolution.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Doi N,Itaya M,Yomo T,Tokura S,Yanagawa Hdoi
10.1016/s0014-5793(96)01522-0subject
Has Abstractpub_date
1997-02-03 00:00:00pages
177-80issue
2-3eissn
0014-5793issn
1873-3468pii
S0014-5793(96)01522-0journal_volume
402pub_type
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