Title: Localization and targeting of the Saccharomyces cerevisiae Kre2p/Mnt1p alpha 1,2-mannosyltransferase to a medial-Golgi compartment Document date: 1995_11_2
ID: q1jx0n0l_36
Snippet: The role of the luminal amino acid residues flanking the Kre2p TMD was examined with fusion protein KD-K. It comprises the Kre2p NH2 terminus, the membrane-spanning domain of DPAP B, the Kre2p stem region lacking the first 36 amino acid residues following the TMD, and the catalytic domain of Kre2p. KD-K was found to be localized in the Golgi complex (Fig. 7) suggesting that neither the deleted stem region nor the TMD is necessary for Golgi retent.....
Document: The role of the luminal amino acid residues flanking the Kre2p TMD was examined with fusion protein KD-K. It comprises the Kre2p NH2 terminus, the membrane-spanning domain of DPAP B, the Kre2p stem region lacking the first 36 amino acid residues following the TMD, and the catalytic domain of Kre2p. KD-K was found to be localized in the Golgi complex (Fig. 7) suggesting that neither the deleted stem region nor the TMD is necessary for Golgi retention in the context of a Kre2p catalytic domain.
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