D 2004

Tissue specific alternative splicing in the gene for AHP5, a histidine-containing phosphotransfer protein from Arabidopsis thaliana

HRADILOVÁ, Jana a Břetislav BRZOBOHATÝ

Základní údaje

Originální název

Tissue specific alternative splicing in the gene for AHP5, a histidine-containing phosphotransfer protein from Arabidopsis thaliana

Autoři

HRADILOVÁ, Jana a Břetislav BRZOBOHATÝ

Vydání

Praha, IV. Mezioborové setkání mladých biologů, biochemiků a chemiků, Chemické listy, s. 282-282, 2004

Nakladatel

Česká společnost chemická

Další údaje

Jazyk

angličtina

Typ výsledku

Stať ve sborníku

Obor

Genetika a molekulární biologie

Stát vydavatele

Česká republika

Utajení

není předmětem státního či obchodního tajemství

Označené pro přenos do RIV

Ano

Organizační jednotka

Přírodovědecká fakulta

ISBN

0009-2770

Klíčová slova anglicky

AHP5; alternative splicing; two-component system; Arabidopsis thaliana
Změněno: 30. 9. 2004 15:37, Mgr. Jana Hradilová, Ph.D.

Anotace

V originále

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, záměr
Název: Genomy a jejich funkce
Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Genomy a jejich funkce