TY - JOUR
T1 - Snapshots of DsbA in Action
T2 - Detection of Proteins in the Process of Oxidative Folding
AU - Kadokura, Hiroshi
AU - Tian, Hongping
AU - Zander, Thomas
AU - Bardwell, James C.A.
AU - Beckwith, Jon
PY - 2004/1/23
Y1 - 2004/1/23
N2 - DsbA, a thioredoxin superfamily member, introduces disulfide bonds into newly translocated proteins. This process is thought to occur via formation of mixed disulfide complexes between DsbA and its substrates. However, these complexes are difficult to detect, probably because of their short-lived nature. Here we show that it is possible to detect such covalent intermediates in vivo by a mutation in DsbA that alters cis proline-151. Further, this mutant allowed us to identify substrates of DsbA. Alteration of the cis proline, highly conserved among thioredoxin superfamily members, may be useful for the detection of substrates and intermediate complexes in other systems.
AB - DsbA, a thioredoxin superfamily member, introduces disulfide bonds into newly translocated proteins. This process is thought to occur via formation of mixed disulfide complexes between DsbA and its substrates. However, these complexes are difficult to detect, probably because of their short-lived nature. Here we show that it is possible to detect such covalent intermediates in vivo by a mutation in DsbA that alters cis proline-151. Further, this mutant allowed us to identify substrates of DsbA. Alteration of the cis proline, highly conserved among thioredoxin superfamily members, may be useful for the detection of substrates and intermediate complexes in other systems.
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U2 - 10.1126/science.1091724
DO - 10.1126/science.1091724
M3 - Article
C2 - 14739460
AN - SCOPUS:1642556877
SN - 0036-8075
VL - 303
SP - 534
EP - 537
JO - Science
JF - Science
IS - 5657
ER -