A new group of plant-specific ATP-dependent DNA ligases identified by protein phylogeny, hydrophobic cluster analysis and 3-dimensional modelling

2005 ◽  
Vol 32 (2) ◽  
pp. 161 ◽  
Author(s):  
Diego Bonatto ◽  
Martin Brendel ◽  
João Antonio Pêgas Henriques

The eukaryotic ATP-dependent DNA ligases comprise a group of orthologous proteins that have distinct roles in DNA metabolism. In contrast with the well-known DNA ligases of animal cells, the DNA ligases of plant cells are poorly described. Until now, only two DNA ligases (I and IV) genes of Arabidopsis thaliana (L.) Heynh were isolated and characterised. Use of the complete genomic sequences of Oryza sativa L. and A. thaliana, as well as the partially assembled genomic data of Medicago truncatula L. and Brassica spp., allowed us to identify a new family of ATP-dependent DNA ligases that are found only in the Viridiplantae kingdom. An in-depth phylogenetic analysis of protein sequences showed that this family composes a distinct clade, which shares a last universal common ancestor with DNA ligases I. In silico sequence studies indicate that these proteins have distinct physico-chemical properties when compared with those of animal and fungal DNA ligases. Moreover, hydrophobic cluster analysis and 3-dimensional modelling allowed us to map two conserved domains within these DNA ligases I-like proteins. Additional data of microsynteny analysis indicate that these DNA ligases I-like genes are linked to the S and SLL2 loci of Brassica spp. and A. thaliana, respectively. Combining the results of all analyses, we propose the creation of the DNA ligases VI (LIG6) family, which is composed by plant-specific DNA ligases.

2000 ◽  
Vol 347 (3) ◽  
pp. 741-747 ◽  
Author(s):  
Isabelle MOUYNA ◽  
Michel MONOD ◽  
Thierry FONTAINE ◽  
Bernard HENRISSAT ◽  
Barbara LÉCHENNE ◽  
...  

A new family of glycosylphosphatidylinositol-anchored β(1-3)glucanosyltransferases (Gelp), recently identified and characterized in the filamentous fungus Aspergillus fumigatus, showed functional similarity to the Gas/Phr/Epd protein families, which are involved in yeast morphogenesis. Sequence comparisons and hydrophobic cluster analysis (HCA) showed that all the Gas/Phr/Epd/Gel proteins belong to a new family of glycosylhydrolases, family 72. We confirmed by site-directed mutagenesis and biochemical analysis that the two conserved glutamate residues (the putative catalytic residues of this family, as determined by HCA) are involved in the active site of this family of glycosylhydrolases.


1997 ◽  
Vol 235 (1) ◽  
pp. 103-107 ◽  
Author(s):  
Isabelle Callebaut ◽  
Jean-Claude Courvalin ◽  
Howard J. Worman ◽  
Jean-Paul Mornon

1989 ◽  
Vol 11 (4) ◽  
pp. 217-225 ◽  
Author(s):  
E. Raimbaud ◽  
A. Buléon ◽  
S. Perez ◽  
B. Henrissat

Biochimie ◽  
2015 ◽  
Vol 119 ◽  
pp. 244-253 ◽  
Author(s):  
Tristan Bitard-Feildel ◽  
Magdalena Heberlein ◽  
Erich Bornberg-Bauer ◽  
Isabelle Callebaut

1989 ◽  
Vol 7 (3) ◽  
pp. 171
Author(s):  
L. Lemesle-Varloot ◽  
V. Bissery ◽  
A. Morgat ◽  
C. Gaboriaud ◽  
J.P. Mornon

1989 ◽  
Vol 34 (1-6) ◽  
pp. 355-361 ◽  
Author(s):  
J.P. Mornon ◽  
V. Bissery ◽  
C. Gaboriaud ◽  
A. Thomas ◽  
T. Ojasoo ◽  
...  

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