Registro completo de metadatos
| Campo DC | Valor | Lengua/Idioma |
|---|---|---|
| dc.creator | Freire, Miguel Angel | - |
| dc.date | 2017-06-22T17:55:45Z | - |
| dc.date | 2017-06-22T17:55:45Z | - |
| dc.date | 2012-09 | - |
| dc.date | 2017-06-16T15:52:50Z | - |
| dc.date.accessioned | 2019-04-29T15:31:46Z | - |
| dc.date.available | 2019-04-29T15:31:46Z | - |
| dc.date.issued | 2012-09 | - |
| dc.identifier | Freire, Miguel Angel; The Zea mays glycine-rich RNA-binding protein MA16 is bound to a ribonucleotide(s) by a stable linkage; Springer Tokyo; Journal Of Plant Research; 125; 5; 9-2012; 653-660 | - |
| dc.identifier | 0918-9440 | - |
| dc.identifier | http://hdl.handle.net/11336/18658 | - |
| dc.identifier | 1618-0860 | - |
| dc.identifier | CONICET Digital | - |
| dc.identifier | CONICET | - |
| dc.identifier.uri | http://rodna.bn.gov.ar:8080/jspui/handle/bnmm/295850 | - |
| dc.description | Expression of the gene encoding the maize glycine-rich RNA-binding protein MA16 is developmentally regulated and it is involved in environmental stress responses. The MA16 protein shows a wide spectrum of RNA-binding activities. On the basis of in vivo labelling, where a [32P]phosphate label was linked to the MA16 protein, Freire and Pages (Plant Mol Biol 29:797–807, 1995) suggested that the protein may be post-translationally modified by phosphorylation. However, further analysis showed that the [32P]phosphate label was sensitive to different treatments, suggesting that modification distinct from protein phosphorylation might occur in the MA16 protein. Biochemical analysis revealed that this [32P]phosphate labelling was resistant to phenol extraction and denaturing SDS-PAGE but sensitive to micrococcal nuclease, RNase A and RNase T1 treatments. The mobility of [35S] labelled MA16 protein on SDS-PAGE did not significantly changed after the nuclease treatments suggesting that the [32P]phosphate label associated to MA16 protein could be a ribonucleotide or a very short ribonucleotide chain. In addition, immunoprecipitation of labelled extracts showed that the ribonucleotide(s) linked to the MA16 protein was removed by phosphorolytic activity. This activity could be catalysed by a phosphate-dependent ribonuclease. The C-terminus of MA16 protein harbouring a glycine-rich domain was predicted to be an intrinsically disordered region. | - |
| dc.description | Fil: Freire, Miguel Angel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto Multidisciplinario de Biología Vegetal. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas Físicas y Naturales. Instituto Multidisciplinario de Biología Vegetal; Argentina | - |
| dc.format | application/pdf | - |
| dc.format | application/pdf | - |
| dc.language | eng | - |
| dc.publisher | Springer Tokyo | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs10265-012-0476-8 | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s10265-012-0476-8 | - |
| dc.rights | info:eu-repo/semantics/restrictedAccess | - |
| dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | - |
| dc.source | reponame:CONICET Digital (CONICET) | - |
| dc.source | instname:Consejo Nacional de Investigaciones Científicas y Técnicas | - |
| dc.source | instacron:CONICET | - |
| dc.subject | EXOSOME | - |
| dc.subject | EXORIBONUCLEASE | - |
| dc.subject | NUCLEOTIDYLYLATION | - |
| dc.subject | NUCLEUS | - |
| dc.subject | Bioquímica y Biología Molecular | - |
| dc.subject | Ciencias Biológicas | - |
| dc.subject | CIENCIAS NATURALES Y EXACTAS | - |
| dc.title | The Zea mays glycine-rich RNA-binding protein MA16 is bound to a ribonucleotide(s) by a stable linkage | - |
| dc.type | info:eu-repo/semantics/article | - |
| dc.type | info:eu-repo/semantics/publishedVersion | - |
| dc.type | info:ar-repo/semantics/articulo | - |
| Aparece en las colecciones: | CONICET | |
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