Title 대장균 리보스 결합단백질의 신호배열 변이에 대한 숙성체 부위의 회복돌연변이
Author 이영희1,2 · 송택선1 · 김정호1 · 박순희2 * · 박찬규1
Address 1한국과학기술원 생물공학과; 2한국과학기술연구원 부설 유전공학연구소
Bibliography Korean Journal of Microbiology, 29(5),270-277, 1991
DOI
Key Words Intragenic suppressor, Ribose-binding protein, Protein export, E. coli, SecB
Abstract A mutational alteration in the signal sequence of ribose-binding protein (RBP) of Escherichia coli, rbsB103, completely blocks the export of the protein to the periplasm. Intragenic suppressors for this mutation have been selected on minimal medium with ribose as a sole carbon source. Six suppressor mutations were characterized in detail and were found to have single amino acid wubstitution in the mature portion of RBP, which resulted in the mobility shift of the proteins on SDS polyacrylamide gel. Amino acid changes of these suppressors were localized in several peptides which are packed to form the N terminal domain of typical bilobate conformation of RBP. The involvement of SecB, a molecular chaperone, was investigated in the suppression of signal sequence mutation. Translocation efficency was found to be increased by the presence of SecB for all suppressors. It is likely that the folding characteristics of RBP altered by the suppressor mutations affect the affinity of interaction between SecB and RBP.
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