Abstract:A nuclear genomic library of Glycine max generated in Charon 35 was a gift from Dr R. Nagao. A 2.3 kbp long HindIII fragment (AB2.3) was cloned in the high copy plasmid pTZ-19R and the 5' 911 nucleotides were dideoxy-sequenced (Fig. 1). Nucleotides 1 -4 4 code a portion of a transit peptide. Homology block III [3] is located at nucleotides 21-44 and is preceded by a less homologous "interblock" at nucleotides 3 -20. An open reading frame from methionine at nucleotide 45 to a TGA termination codon (nucleotides … Show more
“…Consensus amino acid sequences for Type I and Type II LHC-II proteins were created from all published cab gene sequences, 31 genes from 12 species [6,8,10,11,14,17,20,22,24,25,29,31,32,35,36,38].…”
A cDNA library was constructed from mRNA prepared from light-treated seedlings of Scots pine (Pinus sylvestris L.) and cDNAs for the chlorophyll a/b-binding protein LHC-II were identified using a pea gene as the heterologous probe. Three cDNA clones were sequenced. The deduced amino acid sequences of two of the genes corresponded to Type I and one to Type II LHC-II proteins which were ca. 90% homologous to their angiosperm counterparts. The transit peptides of the Scots pine preLHC-II showed features common to angiosperm transit peptides. The three cDNAs had a 70 to 75% preference for G + C in the third base position. CpG and GpC profiles and degenerate codon position bias suggested that two of the corresponding genes lie within CpG islands.
“…Consensus amino acid sequences for Type I and Type II LHC-II proteins were created from all published cab gene sequences, 31 genes from 12 species [6,8,10,11,14,17,20,22,24,25,29,31,32,35,36,38].…”
A cDNA library was constructed from mRNA prepared from light-treated seedlings of Scots pine (Pinus sylvestris L.) and cDNAs for the chlorophyll a/b-binding protein LHC-II were identified using a pea gene as the heterologous probe. Three cDNA clones were sequenced. The deduced amino acid sequences of two of the genes corresponded to Type I and one to Type II LHC-II proteins which were ca. 90% homologous to their angiosperm counterparts. The transit peptides of the Scots pine preLHC-II showed features common to angiosperm transit peptides. The three cDNAs had a 70 to 75% preference for G + C in the third base position. CpG and GpC profiles and degenerate codon position bias suggested that two of the corresponding genes lie within CpG islands.
The current state of knowledge concerning the expression of the nuclear genes that code the light-harvesting chlorophyll a/b-binding polypeptides of photosystem II is presented. This review covers the structure of these genes, the complex multistep pathway involved in their expression, and the environmental and other factors which regulate their expression. Some of the effects of these factors are mediated, at least in part, at the level of transcription, but other effects can be explained only by the existence of multiple posttranscriptional regulatory steps.
“…These are located within the thylakoid membranes of the chloroplast, and are made up of nuclear-encoded proteins bound to chlorophylls a and b. Genes encoding proteins of the LHCII (Cab) have been sequenced and characterised for a variety of plant species including Brassica, soybean, rice and barley [ 1,2,7,12].However, there is much less sequence information on the LHCI proteins. So far three types of LHCI genes have been analysed: Types I and III were isolated from tomato [9, 11] and Type lI from pine, tomato and petunia [5,10,13].…”
mentioning
confidence: 99%
“…These are located within the thylakoid membranes of the chloroplast, and are made up of nuclear-encoded proteins bound to chlorophylls a and b. Genes encoding proteins of the LHCII (Cab) have been sequenced and characterised for a variety of plant species including Brassica, soybean, rice and barley [ 1,2,7,12].…”
A monoclonal antibody (MAb UB42) is described that binds to thylakoids in pea chloroplasts, as shown by EM-immunogold labelling. The antibody recognised proteins of ca. 23-29 kDa in western blots of a pea leaf homogenate. A cDNA library was prepared from pea epidermal cells in the vector lambda ZAP II, and immunoscreening of the library with UB42 led to the isolation of a clone, pUB42. This was sequenced and had an open reading frame of 269 codons encoding a predicted polypeptide of 28.9 kDa. The sequence showed extensive homology with three closely related polypeptides belonging to a family of chlorophyll a/b-binding proteins from the light harvesting complex of photosystem I (LHCI). Collectively, the results suggest that MAb UB42 recognises an epitope on the type II chlorophyll a/b-binding protein from LHCI and that clone pUB42 encodes this protein.
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