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J. Biol. Chem., Vol. 265, Issue 6, 3324-3331, Feb, 1990
RN Russo, NL Shaper and JH Shaper
We have used S1 and primer extension analysis to demonstrate that the gene
for bovine beta 1----4-galactosyltransferase specifies two sets of mRNA
transcripts of different lengths. The longer mRNA transcripts initiate
upstream of two in-frame ATG codons and encode a protein of 402 amino acids
(long form). The shorter mRNA transcripts initiate between the two in-frame
ATG codons and encode a protein of 389 amino acids (short form). These two
related forms of beta 1----4- galactosyltransferase have an identical large
(358 amino acids), potentially glycosylated, COOH-terminal catalytic
domain, and an identical single transmembrane domain. The only difference
in primary structure between the two forms is that the long form contains
an NH2- terminal extension of 13 amino acids. Thus, bovine beta 1----4-
galactosyltransferase fits the pattern established for murine beta 1----
4-galactosyltransferase (Shaper, N. L., Hollis, G. L., Douglas, J. G.,
Kirsch, I. R., and Shaper, J. H. (1988) J. Biol. Chem. 263, 10420- 10428).
Inspection of the NH2-terminal domain suggests that the long form of the
bovine enzyme, like its murine counterpart, has a functional cleavable
signal sequence which would dictate that the two forms of the
membrane-bound enzyme are oriented in opposite directions. We have tested
this hypothesis by in vitro translation in the absence or presence of dog
pancreas microsomes. In vitro translation of RNA transcripts for the long
and short form of beta 1----4- galactosyltransferase in the absence of
microsomes results in the synthesis of polypeptides with apparent Mr of
44,500 and 43,000, respectively. In vitro translation of each transcript in
the presence of microsomes results in the synthesis of two glycosylated,
endoglycosidase H-sensitive proteins with apparent Mr of 47,500 and 46,000.
These experiments and additional protease protection experiments
demonstrate that the COOH-terminal domain of both the short and the long
form of bovine beta 1----4-galactosyltransferase are translocated into the
microsomal lumen. By extrapolation, both forms of the enzyme are oriented
in vivo as Type II membrane-bound glycoproteins.
Bovine beta 1----4-galactosyltransferase: two sets of mRNA transcripts encode two forms of the protein with different amino-terminal domains. In vitro translation experiments demonstrate that both the short and the long forms of the enzyme are type II membrane-bound glycoproteins
Cell Structure and Function Laboratory, Johns Hopkins University, Baltimore, Maryland 21205.
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