Binding protein (BiP) is the endoplasmic reticulum member of the highl
y conserved HSP70 (heat shock protein 70) family of molecular chaperon
es. We have isolated and characterized two different BiP cDNA clones c
orresponding to genes expressed in immature kernels. These two cDNAs s
hare extensive sequence similarity but map to unlinked loci in the mai
ze genome. A comparison of the aa sequences predicted from the cDNA cl
ones revealed only six aa differences between them. Investigation of g
ene-specifc expression was carried out by RNA gel blot analysis. RNAs
corresponding to both cDNA clones were present in increased amounts in
the endosperm of floury-2 (fl2), Mucronate (Mc) and Defective endospe
rm-B30 (De-B30) maize mutants, which produce abnormal storage protein
s. Similar increases in RNAs corresponding to both probes were detecte
d in cells treated with either of two agents that interfere with prote
in folding, azetidine-2-carboxylic acid (AZC) and tunicamycin. Investi
gation of the genomic complexity of the BiP genes by Southern blot ana
lysis revealed several cross-hybridizing bands. These results are sugg
estive that the BiP genes expressed in endosperm are coordinately regu
lated members of a more complex maize BiP multigene family. (C) 1997 E
lsevier Science B.V.