Literature DB >> 16666074

Translational alterations in maize leaves responding to pathogen infection, paraquat treatment, or heat shock : polysome dissociation and accumulation of a 57 kilodalton protein.

C H Wu1, H L Warren, K Sitaraman, C Y Tsai.   

Abstract

Translational alterations occur in maize (Zea mays L.) leaves stressed by pathogen infection or herbicide paraquat treatment. These translational changes include: (a) dissociation of large polysomes to small polysomes, monosomes, and subunits; (b) a decreased rate of total protein synthesis; and (c) a reduced synthesis of several proteins by polysomes in vitro. The polysome dissociation was neither due to an extraction artifact nor to degradation of RNA by RNase. The protein patterns of polysomes isolated from leaves inoculated with Bipolaris maydis at 6 to 48 hours showed an increase in the intensity of a 57 kilodalton protein. When inoculated with less virulent pathogens, such as B. zeicola, Exserohilum turcicum, or Colletotrichum graminicola, the protein was accumulated in polysomes of leaves at 24 to 48 hours after inoculation. The 57 kilodalton protein was also accumulated in polysomes of maize leaves responding to heat shock or herbicide paraquat treatments. The purified 57 kilodalton protein reassociated with polysomes isolated from healthy leaves and inhibited polysomal translation in vitro. Since the 57 kilodalton protein is rapidly accumulated in maize polysomes in response to various biological and environmental stresses and may affect protein synthesis, it may be involved in translational regulation of maize leaves during stress response.

Entities:  

Year:  1988        PMID: 16666074      PMCID: PMC1054672          DOI: 10.1104/pp.86.4.1323

Source DB:  PubMed          Journal:  Plant Physiol        ISSN: 0032-0889            Impact factor:   8.340


  18 in total

1.  Chromatographic separation of ribonucleases in corn.

Authors:  C M WILSON
Journal:  Biochim Biophys Acta       Date:  1963-02-26

Review 2.  Changes in plant gene expression during stress.

Authors:  G L Matters; J G Scandalios
Journal:  Dev Genet       Date:  1986

3.  The ribosomal proteins of Escherichia coli. I. Purification of the 30S ribosomal proteins.

Authors:  S J Hardy; C G Kurland; P Voynow; G Mora
Journal:  Biochemistry       Date:  1969-07       Impact factor: 3.162

4.  Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

Authors:  U K Laemmli
Journal:  Nature       Date:  1970-08-15       Impact factor: 49.962

5.  Effect of heat shock on ribosome structure: appearance of a new ribosome-associated protein.

Authors:  T W McMullin; R L Hallberg
Journal:  Mol Cell Biol       Date:  1986-07       Impact factor: 4.272

6.  Heat shock causes diverse changes in the phosphorylation of the ribosomal proteins of mammalian cells.

Authors:  I M Kennedy; R H Burdon; D P Leader
Journal:  FEBS Lett       Date:  1984-04-24       Impact factor: 4.124

7.  The wheat embryo cell-free system.

Authors:  A Marcus; D Efron; D P Weeks
Journal:  Methods Enzymol       Date:  1974       Impact factor: 1.600

8.  The anaerobic proteins of maize.

Authors:  M M Sachs; M Freeling; R Okimoto
Journal:  Cell       Date:  1980-07       Impact factor: 41.582

9.  Dissocation and reassembly of polyribosomes in relation to protein synthesis in the soybean root.

Authors:  C Y Lin; J L Key
Journal:  J Mol Biol       Date:  1967-06-14       Impact factor: 5.469

10.  Free messenger ribonucleoprotein complexes of chicken primary muscle cells following modification of protein synthesis by heat-shock treatment.

Authors:  J Bag
Journal:  Eur J Biochem       Date:  1983-09-15
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