DC Field | Value | Language |
dc.contributor.author | Merzendorfer, H | |
dc.contributor.author | Huss, M | |
dc.contributor.author | Schmid, P | |
dc.contributor.author | Harvey, WR | |
dc.contributor.author | Wieczorek, H | |
dc.date.accessioned | 2021-12-23T16:13:56Z | - |
dc.date.available | 2021-12-23T16:13:56Z | - |
dc.date.issued | 1999 | |
dc.identifier.issn | 00219258 | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/10823 | - |
dc.description.abstract | Plasma membrane V-ATPase isolated from midgut and Malpighian tubules of the tobacco hornworm, Manduca sexta, contains a novel prominent 20-kDa polypeptide. Based on N-terminal protein sequencing, we cloned a corresponding cDNA. The deduced hydrophobic protein consisted of 88 amino acids with a molecular mass of only 9.7 kDa. Immunoblots of the recombinant 9.7-kDa polypeptide, using a monoclonal antibody to the 20-kDa polypeptide, confirmed that the correct cDNA had been cloned. The 20-kDa polypeptide is glycosylated, as deduced from lectin staining. Treatment with N-glycosidase A resulted in the appearance of two additional protein bands of 16 and 10 kDa which both were immunoreactive to the 20-kDa polypeptide-specific monoclonal antibody. Thus, extensive N-glycosylation of the novel V-0 subunit M9.7 accounts for half of its molecular mass observed in SDS-polyacrylamide gel electrophoresis. M9.7 exhibits some similarities to the yeast protein Vma21p which resides in the endoplasmic reticulum and is required for the assembly of the V-0 complex. However, as deduced from immunoblots as well as from activities of the V-ATPase and endoplasmic reticulum marker enzymes in different membrane preparations, M9.7 is, in contrast to the yeast polypeptide, a constitutive subunit of the mature plasma membrane V-ATPase of M. sexta. | |
dc.language.iso | en | |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | |
dc.relation.ispartof | JOURNAL OF BIOLOGICAL CHEMISTRY | |
dc.subject | Biochemistry & Molecular Biology | |
dc.subject | ENDOPLASMIC-RETICULUM | |
dc.subject | ESCHERICHIA-COLI | |
dc.subject | MANDUCA-SEXTA MIDGUT | |
dc.subject | PLASMA-MEMBRANE | |
dc.subject | POLYACRYLAMIDE GELS | |
dc.subject | POLYMERASE CHAIN-REACTION | |
dc.subject | PROTON PUMP | |
dc.subject | SECONDARY-STRUCTURE | |
dc.subject | TOBACCO HORNWORM MIDGUT | |
dc.subject | VACUOLAR-TYPE ATPASE | |
dc.title | A novel insect V-ATPase subunit M9.7 is glycosylated extensively | |
dc.type | journal article | |
dc.identifier.doi | 10.1074/jbc.274.24.17372 | |
dc.identifier.isi | ISI:000080780400098 | |
dc.description.volume | 274 | |
dc.description.issue | 24 | |
dc.description.startpage | 17372 | |
dc.description.endpage | 17378 | |
dc.publisher.place | 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 USA | |
dcterms.isPartOf.abbreviation | J. Biol. Chem. | |
dcterms.oaStatus | hybrid | |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.dept | Universität Osnabrück | - |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | MeHa731 | - |
crisitem.author.netid | HuMa001 | - |
crisitem.author.netid | WiHe990 | - |