Post-translational GPI lipid anchor modification of proteins in kingdoms of life: analysis of protein sequence data from complete genomes

被引:141
作者
Eisenhaber, B
Bork, P
Eisenhaber, F
机构
[1] Res Inst Mol Pathol, A-1030 Vienna, Austria
[2] Max Delbruck Ctr Mol Med, D-13122 Berlin, Germany
[3] European Mol Biol Lab, D-69012 Heidelberg, Germany
来源
PROTEIN ENGINEERING | 2001年 / 14卷 / 01期
关键词
genome annotation; GPI lipid anchor attachment; GPI modification prediction; post-translational modification; transamidase complex;
D O I
10.1093/protein/14.1.17
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
To investigate the occurrence of glycosylphosphatidylinositol (GPI) lipid anchor modification in various taxonomic ranges, potential substrate proteins have been searched for in completely sequenced genomes. We applied the big-pi predictor for the recognition of propeptide cleavage and anchor attachment sites with a new, generalized analytical form of the extreme-value distribution for evaluating false-positive prediction rates. (i) We find that GPI modification is present among lower and higher Eukaryota (similar to0.5% of all proteins) but it seems absent in all eubacterial and three archaeobacterial species studied. Four other archaean genomes appear to encode such a fraction of substrate proteins (in the range of eukaryots) that they cannot be explained as false-positive predictions. This result supports the possible existence of GPI anchor modification in an archaean subgroup. (ii) The frequency of GPI-modified proteins on various chromosomes of a given eukaryotic species is different. (iii) Lists of potentially GPI-modified proteins in complete genomes with their predicted cleavage sites are available at http://mendel.imp.univie.ac.at/gpi/gpi_genomes.html. (iv) Orthologues of known transamidase subunits have been found only for Eukarya. Inconsistencies in domain structure among homologues some of which may indicate sequencing errors are described. We present a refined model of the transamidase complex.
引用
收藏
页码:17 / 25
页数:9
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