TY - JOUR
T1 - Divergent Hsc70 binding properties of mitochondrial and cytosolic aspartate aminotransferase
T2 - Implications for their segregation to different cellular compartments
AU - Artigues, Antonio
AU - Crawford, Douglas L.
AU - Iriarte, Ana
AU - Martinez-Carrion, Marino
N1 - Copyright:
Copyright 2007 Elsevier B.V., All rights reserved.
PY - 1998/12/11
Y1 - 1998/12/11
N2 - Cytosolic Hsc70 discriminates between the homologous mitochondrial and cytosolic isozymes of aspartate aminotransferase, binding exclusively the mitochondrial form. By screening a library of synthetic peptides spanning the sequence of the mitochondrial enzyme, we have identified binding sites in this polypeptide that interact with Hsc70. These potential binding sites are scattered over the entire sequence and map to secondary structure elements, particularly the α-helix, that are partly exposed on the surface of the native protein. Several peptides corresponding to analogous positions in the cytosolic enzyme sequence do not bind to Hsc70. Phylogenetic analyses suggest that Hsc70 binding sequences have diverged as a consequence of biochemical specialization ensuring differential interaction of each isozyme with the cellular machinery in charge of protein folding and translocation.
AB - Cytosolic Hsc70 discriminates between the homologous mitochondrial and cytosolic isozymes of aspartate aminotransferase, binding exclusively the mitochondrial form. By screening a library of synthetic peptides spanning the sequence of the mitochondrial enzyme, we have identified binding sites in this polypeptide that interact with Hsc70. These potential binding sites are scattered over the entire sequence and map to secondary structure elements, particularly the α-helix, that are partly exposed on the surface of the native protein. Several peptides corresponding to analogous positions in the cytosolic enzyme sequence do not bind to Hsc70. Phylogenetic analyses suggest that Hsc70 binding sequences have diverged as a consequence of biochemical specialization ensuring differential interaction of each isozyme with the cellular machinery in charge of protein folding and translocation.
UR - http://www.scopus.com/inward/record.url?scp=0032509352&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032509352&partnerID=8YFLogxK
U2 - 10.1074/jbc.273.50.33130
DO - 10.1074/jbc.273.50.33130
M3 - Article
C2 - 9837879
AN - SCOPUS:0032509352
VL - 273
SP - 33130
EP - 33134
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 50
ER -