"Development and Characterization of Genomic Resources for a Non-Model Marine Teleost, the Red Snapper (Lutjanus campechanus, Lutjanidae): Construction of a High-Density Linkage Map, Anchoring of Genome Contigs and Comparative Genomic Analysis"

2019 ◽  
Author(s):  
Adrienne Elise Norrell ◽  
Kenneth L. Jones ◽  
Eric Saillant
Keyword(s):  
Linkage Map ◽  
Genomic Analysis ◽  
Comparative Genomic Analysis ◽  
Red Snapper ◽  
Comparative Genomic ◽  
Marine Teleost ◽  
Lutjanus Campechanus ◽  
Genomic Resources ◽  
High Density Linkage Map

A combined AFLP and microsatellite linkage map and pilot comparative genomic analysis of European sea bassDicentrarchus labraxL.

2008 ◽  
Vol 39 (6) ◽  
pp. 623-634 ◽  
Author(s):  
D. A. Chistiakov ◽  
C. S. Tsigenopoulos ◽  
J. Lagnel ◽  
Y.-M. Guo ◽  
B. Hellemans ◽  
...  
Keyword(s):  
Linkage Map ◽  
Genomic Analysis ◽  
Comparative Genomic Analysis ◽  
Comparative Genomic ◽  
Microsatellite Linkage

scholarly journals Biochemical and Phylogenetic Characterization of a Novel Diaminopimelate Biosynthesis Pathway in Prokaryotes Identifies a Diverged Form of ll-Diaminopimelate Aminotransferase

2008 ◽  
Vol 190 (9) ◽  
pp. 3256-3263 ◽  
Author(s):  
André O. Hudson ◽  
Charles Gilvarg ◽  
Thomas Leustek
Keyword(s):  
Genomic Analysis ◽  
Direct Conversion ◽  
Amino Acid Identity ◽  
Comparative Genomic Analysis ◽  
Lysine Biosynthesis ◽  
Comparative Genomic ◽  
Biosynthesis Pathway ◽  
Acid Identity ◽  
Phylogenetic Characterization

ABSTRACT A variant of the diaminopimelate (DAP)-lysine biosynthesis pathway uses an ll-DAP aminotransferase (DapL, EC 2.6.1.83) to catalyze the direct conversion of l-2,3,4,5-tetrahydrodipicolinate to ll-DAP. Comparative genomic analysis and experimental verification of DapL candidates revealed the existence of two diverged forms of DapL (DapL1 and DapL2). DapL orthologs were identified in eubacteria and archaea. In some species the corresponding dapL gene was found to lie in genomic contiguity with other dap genes, suggestive of a polycistronic structure. The DapL candidate enzymes were found to cluster into two classes sharing approximately 30% amino acid identity. The function of selected enzymes from each class was studied. Both classes were able to functionally complement Escherichia coli dapD and dapE mutants and to catalyze ll-DAP transamination, providing functional evidence for a role in DAP/lysine biosynthesis. In all cases the occurrence of dapL in a species correlated with the absence of genes for dapD and dapE representing the acyl DAP pathway variants, and only in a few cases was dapL coincident with ddh encoding meso-DAP dehydrogenase. The results indicate that the DapL pathway is restricted to specific lineages of eubacteria including the Cyanobacteria, Desulfuromonadales, Firmicutes, Bacteroidetes, Chlamydiae, Spirochaeta, and Chloroflexi and two archaeal groups, the Methanobacteriaceae and Archaeoglobaceae.

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