The Caenorhabditis elegans RAD51 homolog is transcribed into two alternative mRNAs potentially encoding proteins of different sizes.
In prokaryotes, the RecA protein plays a pivotal role in homologous recombination, catalyzing the transfer of a single DNA strand into an homologous molecule. Structural homologs of the bacterial RecA protein, called Rad51, have been found in different eukaryotes (from yeast to man), suggesting a certain level of conservation in recombination pathways among living organisms. We have cloned the homolog of RAD51 in Caenorhabditis elegans. The CeRAD51 gene is transcribed into two alternative mRNAs and potentially codes for two proteins of 395 and 357 amino acids in length, respectively. We discuss the evolutionary implications of these findings.
Rinaldo
C
C
International Institute of Genetics and Biophysics-CNR, Naples, Italy.
Ederle
S
S
Rocco
V
V
La Volpe
A
A
D017398:Alternative Splicing; D000595:Amino Acid Sequence; D000818:Animals; D017173:Caenorhabditis elegans / Q000235:genetics*; D029742:Caenorhabditis elegans Proteins; D002874:Chromosome Mapping; D003001:Cloning, Molecular; D004268:DNA-Binding Proteins / Q000235:genetics* / Q000378:metabolism*; D005786:Gene Expression Regulation; D008969:Molecular Sequence Data; D010802:Phylogeny; D012333:RNA, Messenger; D051135:Rad51 Recombinase; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D014158:Transcription, Genetic
D029742:Caenorhabditis elegans Proteins; D004268:DNA-Binding Proteins; D012333:RNA, Messenger; D051135:Rad51 Recombinase; C495148:rad-51 protein, C elegans