Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    ISSN: 1617-4623
    Keywords: Key words eIF3 ; Maize ; Protein synthesis ; Translation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In order to identify genes that are specifically expressed in distinct cell populations of the maize root apex, we have constructed PCR-directed cDNA libraries from microdissected populations of cells, and screened them by differential hybridisation. A meristem-specific cDNA was isolated and characterised. This cDNA, termed ZmeIF3A, encodes a protein homologous to the large subunit of the eukaryotic translation Initiation Factor 3 (eIF3), which is an essential multi-protein complex for the initiation of protein synthesis. The ZmeIF3A protein is most similar to the yeast homologue RPG1, lacking the repeated C-terminal domain characteristic of its mammalian counterparts. However, despite this similarity, it fails to replace the RPG1 protein in complementation experiments on yeast mutants. Analysis of gene expression in situ showed that the ZmeIF3A transcript is expressed in the region of the root meristem surrounding the central stele. ZmeIF3A mRNA is also expressed in the young root, the male inflorescence, and the developing cob and seed. In maize, ZmeIF3A is encoded by one or two genomic sequences. This is the first report on the isolation and characterisation of a cDNA from higher plants that encodes a product homologous to a component of the eIF3 complex.
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
  • 2
    ISSN: 1432-2048
    Keywords: Endosperm ; Protein body ; Protein synthesis (in vitro) ; Secate (storage protein) ; Seed maturation ; Storage protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The synthesis and deposition of the endosperm storage proteins of rye, usually termed secalins, has been studied. The rate of accumulation of secalin in developing rye grain was at a maximum between 3 and 5 weeks after anthesis. Some changes in the proportions of the four major groups of secalin polypeptides were observed during maturation, notably an increase in γ-secalins of Mr 75k and a decrease in ω-secalins. In-vitro translation of mRNA fractions prepared from 4-week-old endosperms showed that secalin polypeptides were synthesised on membrane-bound polysomes. The secalin products were identified by their mobilities on SDS-PAGE and their relative incorporation of radioactive lysine, glycine, proline, leucine and methionine. Protein bodies prepared by sucrose density ultracentrifugation contained reduced amounts of γ-secalins of Mr 40k and ω-secalins compared with the total secalin fraction, but these components were present in the expected amounts when 1.0 M NaCl was added to the buffers. Treatment of the protein bodies with proteinase-k resulted in the digestion of their contents regardless of the presence of NaCl, indicating that the surrounding membrane was incomplete. It was concluded that the NaCl reduced the loss of secalins from the protein bodies by decreasing secalin solubility rather than by affecting the integrity of the protein body membrane. The results reported for the synthesis and deposition of secalins are consistent with the results of previous studies on the prolamins of wheat and barley.
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...