Isolation and characterization of CAJ1, a novel yeast homolog of dnaJ.
A novel member of the Escherichia coli dnaJ family, designated CAJ1, was isolated from a yeast expression library using antiserum against a yeast calmodulin-binding fraction. Although CAJ1 contains neither a Gly-rich region nor a Cys-rich repeat, as are found in other DnaJ relatives, it contains a leucine zipper-like motif.
Mukai
H
H
Department of Pharmacology, Kobe University School of Medicine, Japan.
Shuntoh
H
H
Chang
C D
CD
Asami
M
M
Ueno
M
M
Suzuki
K
K
Kuno
T
T
D000595:Amino Acid Sequence; D002148:Calmodulin-Binding Proteins / Q000235:genetics*; D003001:Cloning, Molecular; D029968:Escherichia coli Proteins; D005656:Fungal Proteins / Q000235:genetics*; D050956:HSP40 Heat-Shock Proteins; D006360:Heat-Shock Proteins / Q000235:genetics*; D015151:Immunoblotting; D008969:Molecular Sequence Data; D012441:Saccharomyces cerevisiae / Q000235:genetics*; D029701:Saccharomyces cerevisiae Proteins; D017386:Sequence Homology, Amino Acid
C088621:CAJ1 protein, S cerevisiae; D002148:Calmodulin-Binding Proteins; C494635:DnaJ protein, E coli; D029968:Escherichia coli Proteins; D005656:Fungal Proteins; D050956:HSP40 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D029701:Saccharomyces cerevisiae Proteins