Hsp70 chaperones assist a large variety of protein
folding processes in the cell by transient association
with short peptide segments of proteins. The substrate
binding and release cycle is driven by the
switching between the low affinity ATP bound state
and the high affinity ADP bound state of Hsp70. Considerable
progress has been made recently by the
identification of in vivo substrates for the Escherichia
coli homolog, DnaK, and the molecular mechanisms
which govern the DnaK-substrate interactions. Here
we review the processes that generate DnaK substrates
in vivo and the properties of these substrates,
and we describe insights gained from structural and
kinetic analysis of DnaK-substrate interaction.
Biological Chemistry keeps you up-to-date with the latest advances in the molecular life sciences. The journal publishes Research Articles, Short Communications, Reviews and Minireviews. Areas include: general biochemistry/pathobiochemistry, structural biology, molecular and cellular biology, genetics and epigenetics, virology, molecular medicine, plant molecular biology/biochemistry and novel experimental methodologies.