EC Number   |
Protein Variants |
Reference |
|---|
   7.4.2.3 | E240A/V241A |
the mutation is supposed to affect both a cluster of charge interactions with Lys546 and Arg437 of the mtHsp70 substrate-binding domain, as well as hydrophobic interactions at the interface between the two Hsp70 domains, e.g. Ala542 within alpha-helix A of the substrate-binding domain. Lethal mutation due to a defect in allosteric regulation, phenotype, overview. No complementation of a ssc1 null mutant |
698945 |
| 7.4.2.3 | more |
a T-DNA insertion line for cpHsc70-1 DELTAcpHsc70-1 has variegated cotyledons, malformed leaves, growth retardation, impaired root growth and sensitivity to heat shock treatment. In addition, under stress conditions, the mutant exhibits unusual sepals, and malformed flowers |
713335 |
| 7.4.2.3 | more |
construction of chimera of protein with yeast mtHsp70, alpha-helices A and B of the peptide binding domain of mtHsp70 are required to transmit the nucleotide state of the ATPase domain to the peptide domain in yeast mitochondria |
656108 |
| 7.4.2.3 | more |
construction of chimera of protein with yeast mtHsp70, alpha-helices A and B of the peptide binding domain of mtHsp70 are required to transmit the nucleotide state of the ATPase domain to the peptide domain. Tim44 is proposed to coordinate the binding of mtHsp70 to the incoming preprotein and the subsequent release of the mtHsp70-preprotein complex from the translocase of the inner membrane |
656108 |
| 7.4.2.3 | more |
construction of fusion proteins consisting of a mitochondrial presequence containing the first mtHsp70 binding site, a spacer sequence containing an Hsp70 avoidance segment followed by the second mtHsp70 binding site, and different folded mature domains. Analysis of the dependence of the import rates of those fusion proteins on the lengths of Hsp70 avoidance segments, overview. Import of radiolabeled fusion proteins into isolated Saccharomyces cerevisiae mitochondria |
698809 |
| 7.4.2.3 | more |
cpHsc70-1/cpHsc70-2 double mutants are lethal |
713335 |
| 7.4.2.3 | more |
generation of specific mtHsp70 mutations located within or close to the interface between the nucleotide-binding and the substrate-binding domains. Mitochondria isolated from mtHsp70 mutants display severely reduced import efficiencies in vitro. Two of the mutants exhibit strong growth defects in vivo and are significantly impaired in the generation of an inward-directed, ATP-dependent import force on precursor proteins in transit. Mutants show defects in the transfer of conformational signals to the substrate-binding domain, resulting in a prolonged and enhanced interaction with imported substrate proteins. Furthermore, interference with the allosteric mechanism results in defects of translocation-specific partner protein interaction |
698945 |
| 7.4.2.3 | more |
recombinant GST-tagged mortalin/mtHsp70 deletion mutants, which demonstrate binding of mortalin via its N-terminal region |
667512 |
| 7.4.2.3 | N175A/D176A |
the mutation abolishes a salt bridge that is formed between Asp176 of the nucleotide-binding domain and Lys544 of the substrate-binding domain. The mutant shows a temperature-sensitive phenotype with defect growth at 30°C due to a defect in allosteric regulation, phenotype, overview. No complementation of a ssc1 null mutant |
698945 |
| 7.4.2.3 | Y173A |
residue Tyr173, that is exposed on the molecular surface and located close to both the nucleotide-binding site and the putative domain interface. The mutant displays normal growth that is indistinguishable from cells expressing wild-type Ssc1. Complementation of a ssc1 null mutant |
698945 |
