A novel insect V-ATPase subunit M9.7 is glycosylated extensively

DC FieldValueLanguage
dc.contributor.authorMerzendorfer, H
dc.contributor.authorHuss, M
dc.contributor.authorSchmid, P
dc.contributor.authorHarvey, WR
dc.contributor.authorWieczorek, H
dc.date.accessioned2021-12-23T16:13:56Z-
dc.date.available2021-12-23T16:13:56Z-
dc.date.issued1999
dc.identifier.issn00219258
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/10823-
dc.description.abstractPlasma 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.isoen
dc.publisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
dc.relation.ispartofJOURNAL OF BIOLOGICAL CHEMISTRY
dc.subjectBiochemistry & Molecular Biology
dc.subjectENDOPLASMIC-RETICULUM
dc.subjectESCHERICHIA-COLI
dc.subjectMANDUCA-SEXTA MIDGUT
dc.subjectPLASMA-MEMBRANE
dc.subjectPOLYACRYLAMIDE GELS
dc.subjectPOLYMERASE CHAIN-REACTION
dc.subjectPROTON PUMP
dc.subjectSECONDARY-STRUCTURE
dc.subjectTOBACCO HORNWORM MIDGUT
dc.subjectVACUOLAR-TYPE ATPASE
dc.titleA novel insect V-ATPase subunit M9.7 is glycosylated extensively
dc.typejournal article
dc.identifier.doi10.1074/jbc.274.24.17372
dc.identifier.isiISI:000080780400098
dc.description.volume274
dc.description.issue24
dc.description.startpage17372
dc.description.endpage17378
dc.publisher.place9650 ROCKVILLE PIKE, BETHESDA, MD 20814 USA
dcterms.isPartOf.abbreviationJ. Biol. Chem.
dcterms.oaStatushybrid
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptUniversität Osnabrück-
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.deptidfb05-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidMeHa731-
crisitem.author.netidHuMa001-
crisitem.author.netidWiHe990-
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