HRADILOVÁ, Jana a Břetislav BRZOBOHATÝ. TISSUE SPECIFIC ALTERNATIVE SPLICING IN THE GENE FOR AHP5, A HISTIDINE-CONTAINING PHOSPHOTRANSFER PROTEIN FROM ARABIDOPSIS THALIANA. In VIII.Pracovní setkání biochemik a molekulárních biolog. 1. vyd. Brno: Masarykova univerzita v Brn, 2004, s. 25-26. ISBN 80-210-3321-5.
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Základní údaje
Originální název TISSUE SPECIFIC ALTERNATIVE SPLICING IN THE GENE FOR AHP5, A HISTIDINE-CONTAINING PHOSPHOTRANSFER PROTEIN FROM ARABIDOPSIS THALIANA
Název anglicky TISSUE SPECIFIC ALTERNATIVE SPLICING IN THE GENE FOR AHP5, A HISTIDINE-CONTAINING PHOSPHOTRANSFER PROTEIN FROM ARABIDOPSIS THALIANA
Autoři HRADILOVÁ, Jana (203 Česká republika) a Břetislav BRZOBOHATÝ (203 Česká republika, garant).
Vydání 1. vyd. Brno, VIII.Pracovní setkání biochemik a molekulárních biolog, od s. 25-26, 2 s. 2004.
Nakladatel Masarykova univerzita v Brn
Další údaje
Originální jazyk čeština
Typ výsledku Stať ve sborníku
Obor Genetika a molekulární biologie
Stát vydavatele Česká republika
Utajení není předmětem státního či obchodního tajemství
Kód RIV RIV/00216224:14310/04:00010100
Organizační jednotka Přírodovědecká fakulta
ISBN 80-210-3321-5
Klíčová slova anglicky ALTERNATIVE SPLICING; PHOSPHOTRANSFER PROTEIN; ARABIDOPSIS THALIANA
Štítky alternative splicing, Arabidopsis thaliana, PHOSPHOTRANSFER PROTEIN
Změnil Změnila: Mgr. Jana Hradilová, Ph.D., učo 21324. Změněno: 5. 10. 2004 14:52.
Anotace
A multistep two-component system is involved in signal transduction in Arabidopsis and consists of a sensory histidine kinase, a phosphotransfer factor and a response regulator. Factors with histidine-containing phosphotransfer domains (AHPs) transfer the phosphoryl group from membrane localised receptor (histidine kinases) to effectors (response regulators) localised in the nucleus. Five AHPs have been identified in Arabidopsis. AHPs are small proteins (14,5 18 kDa), with a predicted acidic isoeletric point (5.53.9) and a typical phosphotransfer domain, including the conserved sequence XHQXKGSSXS. AHP5 comprises six exons and five introns. RNA was prepared using Trizol reagent from different plant tissues: leaves, roots, shoot, flowers, siliques and seedlings. Using RT-PCR we detected two products (AHP5s and AHP5l). Following sequencing, the second intron was found intact at position 211 bp in the longer product (AHP5l). Real time RT-PCR showed that the ratio between spliced and nonspliced products is in tested tissues significant different. Other AHPs (AHP1, AHP2, AHP3 and AHP4) were established to be normally spliced. AHP5l comprises two open reading frames, and in the longer of them the phosphotransfer domain is preserved intact as the original reading frame is not altered. This protein has a predicted molecular mass of 11.7kDa and the putative isoeletric point is 7.72.
Anotace anglicky
A multistep two-component system is involved in signal transduction in Arabidopsis and consists of a sensory histidine kinase, a phosphotransfer factor and a response regulator. Factors with histidine-containing phosphotransfer domains (AHPs) transfer the phosphoryl group from membrane localised receptor (histidine kinases) to effectors (response regulators) localised in the nucleus. Five AHPs have been identified in Arabidopsis. AHPs are small proteins (14,5 18 kDa), with a predicted acidic isoeletric point (5.53.9) and a typical phosphotransfer domain, including the conserved sequence XHQXKGSSXS. AHP5 comprises six exons and five introns. RNA was prepared using Trizol reagent from different plant tissues: leaves, roots, shoot, flowers, siliques and seedlings. Using RT-PCR we detected two products (AHP5s and AHP5l). Following sequencing, the second intron was found intact at position 211 bp in the longer product (AHP5l). Real time RT-PCR showed that the ratio between spliced and nonspliced products is in tested tissues significant different. Other AHPs (AHP1, AHP2, AHP3 and AHP4) were established to be normally spliced. AHP5l comprises two open reading frames, and in the longer of them the phosphotransfer domain is preserved intact as the original reading frame is not altered. This protein has a predicted molecular mass of 11.7kDa and the putative isoeletric point is 7.72.
Návaznosti
MSM 143100008, záměrNázev: Genomy a jejich funkce
Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Genomy a jejich funkce
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