TY - JOUR
T1 - Identification of AglE, a second glycosyltransferase involved in N glycosylation of the Haloferax volcanii S-layer glycoprotein
AU - Abu-Qarn, Mehtap
AU - Giordano, Assunta
AU - Battaglia, Francesca
AU - Trauner, Andrej
AU - Hitchen, Paul G.
AU - Morris, Howard R.
AU - Dell, Anne
AU - Eichler, Jerry
PY - 2008/5/1
Y1 - 2008/5/1
N2 - Archaea, like Eukarya and Bacteria, are able to N glycosylate select protein targets. However, in contrast to relatively advanced understanding of the eukaryal N glycosylation process and the information being amassed on the bacterial process, little is known of this posttranslational modification in Archaea. Toward remedying this situation, the present report continues ongoing efforts to identify components involved in the N glycosylation of the Haloferax volcanii S-layer glycoprotein. By combining gene deletion together with mass spectrometry, AglE, originally identified as a homologue of murine Dpm1, was shown to play a role in the addition of the 190-Da sugar subunit of the novel pentasaccharide decorating the S-layer glycoprotein. Topological analysis of an AglE-based chimeric reporter assigns AglE as an integral membrane protein, with its N terminus and putative active site facing the cytoplasm. These finding, therefore, contribute to the developing picture of the N glycosylation pathway in Archaea.
AB - Archaea, like Eukarya and Bacteria, are able to N glycosylate select protein targets. However, in contrast to relatively advanced understanding of the eukaryal N glycosylation process and the information being amassed on the bacterial process, little is known of this posttranslational modification in Archaea. Toward remedying this situation, the present report continues ongoing efforts to identify components involved in the N glycosylation of the Haloferax volcanii S-layer glycoprotein. By combining gene deletion together with mass spectrometry, AglE, originally identified as a homologue of murine Dpm1, was shown to play a role in the addition of the 190-Da sugar subunit of the novel pentasaccharide decorating the S-layer glycoprotein. Topological analysis of an AglE-based chimeric reporter assigns AglE as an integral membrane protein, with its N terminus and putative active site facing the cytoplasm. These finding, therefore, contribute to the developing picture of the N glycosylation pathway in Archaea.
UR - http://www.scopus.com/inward/record.url?scp=42549147096&partnerID=8YFLogxK
U2 - 10.1128/JB.00056-08
DO - 10.1128/JB.00056-08
M3 - Article
C2 - 18310347
AN - SCOPUS:42549147096
SN - 0021-9193
VL - 190
SP - 3140
EP - 3146
JO - Journal of Bacteriology
JF - Journal of Bacteriology
IS - 9
ER -