Divergent Hsc70 binding properties of mitochondrial and cytosolic aspartate aminotransferase

Implications for their segregation to different cellular compartments

Antonio Artigues, Douglas L Crawford, Ana Iriarte, Marino Martinez-Carrion

Research output: Contribution to journalArticle

14 Citations (Scopus)

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 languageEnglish
Pages (from-to)33130-33134
Number of pages5
JournalJournal of Biological Chemistry
Volume273
Issue number50
DOIs
StatePublished - Dec 11 1998
Externally publishedYes

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Mitochondrial Aspartate Aminotransferase
Aspartate Aminotransferases
Isoenzymes
Binding Sites
Protein folding
Peptide Library
Peptides
Protein Folding
Protein Transport
Enzymes
Machinery
Screening
Membrane Proteins

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 journalArticle

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