A complete cDNA encoding y-tubulin protein from Anemia phyllitidis is presented. The deduced amino acid sequence shows an average similarity of 81-86~o to known y-tubulin genes from insects, mammals and fungi. Northern blots indicate the existence of transcripts of ca. 1.9 kb which are expressed dur
Sequence of a cDNA encoding nitrite reductase from the tree Betula pendula and identification of conserved protein regions
โ Scribed by Friemann, Andreas ;Brinkmann, Klaus ;Hachtel, Wolfgang
- Publisher
- Springer
- Year
- 1992
- Tongue
- English
- Weight
- 789 KB
- Volume
- 231
- Category
- Article
- ISSN
- 0026-8925
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โฆ Synopsis
The sequence of an mRNA encoding nitrite reductase (NiR, EC 1.7.7.1.) from the tree Betula pendula was determined. A cDNA library constructed from leaf poly(A)+ mRNA was screened with an oligonucleotide probe deduced from NiR sequences from spinach and maize. A 2.5 kb cDNA was isolated that hybridized to an mRNA, the steady-state level of which increased markedly upon induction with nitrate. The nucleotide sequence of the cDNA contains a reading frame encoding a protein of 583 amino acids that reveals 79% identity with NiR from spinach. The transit peptide of the NiR precursor from birch was determined to be 22 amino acids in size by sequence comparison with NiR from spinach and maize and is the shortest transit peptide reported so far. A graphical evaluation of identities found in the NiR sequence alignment revealed nine well conserved sections each exceeding ten amino acids in size. Sequence comparisons with related redox proteins identified essential residues involved in cofactor binding. A putative binding site for ferredoxin was found in the N-terminal half of the protein.
๐ SIMILAR VOLUMES
The DNA sequence was determined for the Azospirillum brasilense nifH gene and part of the nifD gene. The nifH gene is 885 bp long and encodes 293 amino acid residues. The region upstream of the nifH open reading frame contains a putative promoter whose sequence shows perfect homology with promoters