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Article: Genomic analysis of G protein γ subunits in human and mouse - The relationship between conserved gene structure and G protein βγ dimer formation

TitleGenomic analysis of G protein γ subunits in human and mouse - The relationship between conserved gene structure and G protein βγ dimer formation
Authors
Issue Date2006
PublisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/cellsig
Citation
Cellular Signalling, 2006, v. 18 n. 2, p. 194-201 How to Cite?
AbstractAnalysis of the genomic sequences, cDNAs and expressed sequence tags (ESTs) in human and mouse for the 12 genes of the γ subunits of the heterotrimeric G proteins has allowed us to identify the common versus unique elements of the organization and expression of the members of this important gene family. All of the G protein γ subunit genes are organized around two coding exons, each containing about 100 nucleotides coding for 30-40 amino acids. These two exons each correspond to a functional domain of the protein, which interestingly appears to impose constraints on both the structure of the protein and the structure of the gene. There is large variation in the intron size between these two coding exons, the number and size of 5' and 3' UTRs, and the overall size of the genes. There is general but not absolute conservation in the size and structure of these genes between humans and mice. Alternative splicing and potential differential promoter usage were detected for several Gγ subunits, indicating possible differential regulation in expression. Only for Gγ10, however, did we find an alternative coding transcript. This alternative transcript appears to code for a hybrid protein containing a DnaJ domain in place of its Gγ exon 1 domain, joined to the Gγ10 second exon domain. The predicted mRNA is expressed in humans, and the protein coded by it is readily translated in vitro. This protein does not form a functional G protein βγ dimer, but it could generate a chaperone-like protein related to its DNA-J domain. These studies suggest that alternative splicing is not a prominent mechanism for generating G protein subunit diversity from within the human or mouse genomes. Instead, each of the known 12 γ subunit genes generate transcripts with one prevalent protein. © 2005 Elsevier Inc. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/170349
ISSN
2015 Impact Factor: 4.191
2015 SCImago Journal Rankings: 2.289
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorYang, Wen_US
dc.contributor.authorHildebrandt, JDen_US
dc.date.accessioned2012-10-30T06:07:43Z-
dc.date.available2012-10-30T06:07:43Z-
dc.date.issued2006en_US
dc.identifier.citationCellular Signalling, 2006, v. 18 n. 2, p. 194-201en_US
dc.identifier.issn0898-6568en_US
dc.identifier.urihttp://hdl.handle.net/10722/170349-
dc.description.abstractAnalysis of the genomic sequences, cDNAs and expressed sequence tags (ESTs) in human and mouse for the 12 genes of the γ subunits of the heterotrimeric G proteins has allowed us to identify the common versus unique elements of the organization and expression of the members of this important gene family. All of the G protein γ subunit genes are organized around two coding exons, each containing about 100 nucleotides coding for 30-40 amino acids. These two exons each correspond to a functional domain of the protein, which interestingly appears to impose constraints on both the structure of the protein and the structure of the gene. There is large variation in the intron size between these two coding exons, the number and size of 5' and 3' UTRs, and the overall size of the genes. There is general but not absolute conservation in the size and structure of these genes between humans and mice. Alternative splicing and potential differential promoter usage were detected for several Gγ subunits, indicating possible differential regulation in expression. Only for Gγ10, however, did we find an alternative coding transcript. This alternative transcript appears to code for a hybrid protein containing a DnaJ domain in place of its Gγ exon 1 domain, joined to the Gγ10 second exon domain. The predicted mRNA is expressed in humans, and the protein coded by it is readily translated in vitro. This protein does not form a functional G protein βγ dimer, but it could generate a chaperone-like protein related to its DNA-J domain. These studies suggest that alternative splicing is not a prominent mechanism for generating G protein subunit diversity from within the human or mouse genomes. Instead, each of the known 12 γ subunit genes generate transcripts with one prevalent protein. © 2005 Elsevier Inc. All rights reserved.en_US
dc.languageengen_US
dc.publisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/cellsigen_US
dc.relation.ispartofCellular Signallingen_US
dc.subject.meshAlternative Splicingen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshChromosome Mappingen_US
dc.subject.meshConserved Sequenceen_US
dc.subject.meshDimerizationen_US
dc.subject.meshExonsen_US
dc.subject.meshGtp-Binding Protein Beta Subunits - Chemistryen_US
dc.subject.meshGtp-Binding Protein Gamma Subunits - Chemistry - Genetics - Metabolismen_US
dc.subject.meshGene Fusionen_US
dc.subject.meshGenomicsen_US
dc.subject.meshHsp40 Heat-Shock Proteins - Geneticsen_US
dc.subject.meshHumansen_US
dc.subject.meshMiceen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshMutant Chimeric Proteins - Genetics - Metabolismen_US
dc.subject.meshPromoter Regions, Geneticen_US
dc.subject.meshRna 3' Polyadenylation Signalsen_US
dc.subject.meshTranscription Initiation Siteen_US
dc.titleGenomic analysis of G protein γ subunits in human and mouse - The relationship between conserved gene structure and G protein βγ dimer formationen_US
dc.typeArticleen_US
dc.identifier.emailYang, W:yangwl@hkucc.hku.hken_US
dc.identifier.authorityYang, W=rp00524en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.cellsig.2005.04.011en_US
dc.identifier.pmid16006100-
dc.identifier.scopuseid_2-s2.0-27344435807en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-27344435807&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume18en_US
dc.identifier.issue2en_US
dc.identifier.spage194en_US
dc.identifier.epage201en_US
dc.identifier.isiWOS:000233330900006-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridYang, W=23101349500en_US
dc.identifier.scopusauthoridHildebrandt, JD=7103100854en_US

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