Please use this identifier to cite or link to this item:
https://doi.org/10.1007/BF00282221
DC Field | Value | |
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dc.title | DPhK-γ, a putative Drosophila kinase with homology to vertebrate phosphorylase kinase γ subunits: molecular characterisation of the gene and phenotypic analysis of loss of function mutants | |
dc.contributor.author | Bahri, S.M. | |
dc.contributor.author | Chia, W. | |
dc.date.accessioned | 2014-11-28T02:50:29Z | |
dc.date.available | 2014-11-28T02:50:29Z | |
dc.date.issued | 1994-09 | |
dc.identifier.citation | Bahri, S.M., Chia, W. (1994-09). DPhK-γ, a putative Drosophila kinase with homology to vertebrate phosphorylase kinase γ subunits: molecular characterisation of the gene and phenotypic analysis of loss of function mutants. MGG Molecular & General Genetics 245 (5) : 588-597. ScholarBank@NUS Repository. https://doi.org/10.1007/BF00282221 | |
dc.identifier.issn | 00268925 | |
dc.identifier.uri | http://scholarbank.nus.edu.sg/handle/10635/111860 | |
dc.description.abstract | Partial and total loss of function mutant alleles of a putative Drosophila homologue (DPhK-γ) of the vertebrate phosphorylase kinase γ-subunit gene have been isolated. DPhK-γ is required in early embryonic processes, such as gastrulation and mesoderm formation; however, defects in these processes are seen only when both the maternal and zygotic components of DPhK-γ expression are eliminated. Loss of zygotic expression alone does not appear to affect normal embryonic and larval development; some pupal lethality is observed but the majority of mutant animals eclose as adults. Many of these adults show defects in their leg musculature (e.g. missing and degenerating muscles), in addition to exhibiting melanised "tumours" on their leg joints. Loss of only the maternal component has no obvious phenotypic consequences. The DPhKγ gene has been cloned and sequenced. It has an open reading frame (ORF) of 1680 by encoding a 560 amino acid protein. The predicted amino acid sequence of DPhK-γ has two conserved domains, the catalytic kinase and calmodulin-binding domains, separated by a linker sequence. The amino acid sequence of DPhK-γ is homologous to that of mammalian PhK-γ proteins but differs in the length and amino acid composition of its linker sequence. The expression of DPhK-γ mRNA is developmentally regulated. We discuss the implications of these observations. © 1994 Springer-Verlag. | |
dc.description.uri | http://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1007/BF00282221 | |
dc.source | Scopus | |
dc.subject | Drosophila | |
dc.subject | Kinase | |
dc.subject | Maternal effect | |
dc.subject | Phosphorylase kinase γ gene | |
dc.type | Article | |
dc.contributor.department | INSTITUTE OF MOLECULAR & CELL BIOLOGY | |
dc.description.doi | 10.1007/BF00282221 | |
dc.description.sourcetitle | MGG Molecular & General Genetics | |
dc.description.volume | 245 | |
dc.description.issue | 5 | |
dc.description.page | 588-597 | |
dc.description.coden | MGGEA | |
dc.identifier.isiut | A1994PX72000007 | |
Appears in Collections: | Staff Publications |
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