Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 33130-33134 |
| Number of pages | 5 |
| Journal | Journal of Biological Chemistry |
| Volume | 273 |
| Issue number | 50 |
| DOIs | |
| State | Published - Dec 11 1998 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
Cite this
Divergent Hsc70 binding properties of mitochondrial and cytosolic aspartate aminotransferase : Implications for their segregation to different cellular compartments. / Artigues, Antonio; Crawford, Douglas L; Iriarte, Ana; Martinez-Carrion, Marino.
In: Journal of Biological Chemistry, Vol. 273, No. 50, 11.12.1998, p. 33130-33134.Research output: Contribution to journal › Article
}
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
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.
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U2 - 10.1074/jbc.273.50.33130
DO - 10.1074/jbc.273.50.33130
M3 - Article
VL - 273
SP - 33130
EP - 33134
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 50
ER -