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Subunit a of proton ATPase F 0 sector is a substrate of the FtsH protease in Escherichia coli
Author(s) -
Akiyama Yoshinori,
Kihara Akio,
Ito Koreaki
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01283-5
Subject(s) - protein subunit , escherichia coli , atpase , translocase , protease , biochemistry , aaa proteins , specificity factor , biology , protein degradation , substrate (aquarium) , enzyme , mutant , chemistry , gene , chromosomal translocation , ecology , rna polymerase
Escherichia coli FtsH is a membrane‐bound ATPase with a proteolytic activity against the SecY subunit of protein translocase. We now report that subunit a of the membrane‐embedded F 0 part of H + ‐ATPase is another substrate of FtsH. Pulse‐chase experiments showed that subunit a is unstable when it alone (without F 0 subunits b and c ) was oversynthesized and that it is stabilized in the ftsH mutants. Selective and ATP‐dependent degradation of subunit a by purified FtsH protein was demonstrated in vitro. These results suggest that FtsH serves as a quality‐control mechanism to avoid potentially harmful accumulation of free subunit a in the membrane.