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Basic characterization of two barley hemA promoter regionsreveals stem-loop structures and suggests a regulatory rolein Poaceae tetrapyrrole biosynthesis

Hansson, Mats LU (2001) In Plant Physiology and Biochemistry 39(2). p.155-160
Abstract
5-Aminolevulinic acid (ALA) is a common biosynthetic intermediate of both chlorophyll and heme. Glutamyl-tRNAGlu reductase, encoded by the hemA gene, is the initial enzyme of ALA biosynthesis. The presence of several hemA genes provides a possible explanation to the ability of plants to meet the different requirement of chlorophyll and heme using a common biosynthetic pathway. In this work, two barley (Hordeum vulgare L.) hemA genes were cloned from chromosomal DNA. The hemA1 and hemA2 genes are located at the long and short arm, respectively, of barley chromosome 5 (1H). Although having 98 % identical coding sequences the promoter regions of hemA1 and hemA2 are very different, which could explain their different expression patterns. The... (More)
5-Aminolevulinic acid (ALA) is a common biosynthetic intermediate of both chlorophyll and heme. Glutamyl-tRNAGlu reductase, encoded by the hemA gene, is the initial enzyme of ALA biosynthesis. The presence of several hemA genes provides a possible explanation to the ability of plants to meet the different requirement of chlorophyll and heme using a common biosynthetic pathway. In this work, two barley (Hordeum vulgare L.) hemA genes were cloned from chromosomal DNA. The hemA1 and hemA2 genes are located at the long and short arm, respectively, of barley chromosome 5 (1H). Although having 98 % identical coding sequences the promoter regions of hemA1 and hemA2 are very different, which could explain their different expression patterns. The first 170 nucleotides of the coding region of both genes contain several inverted repeat regions capable of forming stem-loop structures, which could be involved in the regulation of tetrapyrrole biosynthesis in species belonging to the Poaceae family. (Less)
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organization
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type
Contribution to journal
publication status
published
subject
keywords
5-aminolevulinate, chlorophyll, chromosomal location, glutamyl-tRNAGlu reductase, Hordeum vulgare, inverted repeat, regulation
in
Plant Physiology and Biochemistry
volume
39
issue
2
pages
155 - 160
publisher
Elsevier
external identifiers
  • scopus:0035093957
ISSN
1873-2690
DOI
10.1016/S0981-9428(00)01227-4
language
English
LU publication?
yes
id
a2253680-c0ce-40ff-9238-58455f7e662a (old id 124997)
date added to LUP
2007-07-05 11:57:32
date last changed
2018-05-29 10:04:13
@article{a2253680-c0ce-40ff-9238-58455f7e662a,
  abstract     = {5-Aminolevulinic acid (ALA) is a common biosynthetic intermediate of both chlorophyll and heme. Glutamyl-tRNAGlu reductase, encoded by the hemA gene, is the initial enzyme of ALA biosynthesis. The presence of several hemA genes provides a possible explanation to the ability of plants to meet the different requirement of chlorophyll and heme using a common biosynthetic pathway. In this work, two barley (Hordeum vulgare L.) hemA genes were cloned from chromosomal DNA. The hemA1 and hemA2 genes are located at the long and short arm, respectively, of barley chromosome 5 (1H). Although having 98 % identical coding sequences the promoter regions of hemA1 and hemA2 are very different, which could explain their different expression patterns. The first 170 nucleotides of the coding region of both genes contain several inverted repeat regions capable of forming stem-loop structures, which could be involved in the regulation of tetrapyrrole biosynthesis in species belonging to the Poaceae family.},
  author       = {Hansson, Mats},
  issn         = {1873-2690},
  keyword      = {5-aminolevulinate,chlorophyll,chromosomal location,glutamyl-tRNAGlu reductase,Hordeum vulgare,inverted repeat,regulation},
  language     = {eng},
  number       = {2},
  pages        = {155--160},
  publisher    = {Elsevier},
  series       = {Plant Physiology and Biochemistry},
  title        = {Basic characterization of two barley hemA promoter regionsreveals stem-loop structures and suggests a regulatory rolein Poaceae tetrapyrrole biosynthesis},
  url          = {http://dx.doi.org/10.1016/S0981-9428(00)01227-4},
  volume       = {39},
  year         = {2001},
}