A homolog of Escherichia coli RecA in mitochondria of the cellular slime mold Dictyostelium discoideum

Hasegawa, Yasuna; Wakabayashi, Masayuki; Nakamura, Shōgo; Kodaira, Ken-Ichi; Shinohara, Hiroaki; Yasukawa, Hiro

doi:10.1016/j.dnarep.2004.01.014

Cited by 7 publications

(10 citation statements)

References 23 publications

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“…Two types of recA gene, derived from mitochondria and chloroplasts in Streptophyta (plants), and from mitochondrial recA in Dictyostelium spp. (Mycetozoa) (Hasegawa et al, 2004), were added, in addition to their rad51 sequences. A phylogenetic tree was constructed from these nucleotide sequences, as described in Materials and Methods.…”

Section: Resultsmentioning

confidence: 99%

Transposition of insertion sequence IS256Bsu1 in Bacillus subtilis 168 is strictly dependent on recA

et al. 2017

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We developed an insertion sequence transposition detection system called the "jumping cat assay" and applied it to the Bacillus subtilis chromosome using IS256Bsu1 derived from B. subtilis natto. The high frequency of transposition enabled us to explore host factors; combining the assay and genetic analyses revealed that recA is essential for the transposition of IS256Bsu1. Detailed analyses using various domain mutants of recA demonstrated that this essentiality is not related to the function of recA in homologous recombination. Instead, the ATP binding and hydrolysis function seemed to be crucial for IS transposition. To elucidate the role of recA, we focused on the muB gene of the enterobacteriophage Mu. Based on information from the NCBI Conserved Domain Database, both MuB and RecA belong to the P-loop dNTPase superfamily. Further experiments revealed that muB complements the transposition-defective phenotype of a recA deletant, although it could not rescue UV sensitivity. These results suggest that recA shares a common function with muB that helps the transposition of IS256Bsu1 in B. subtilis.

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Section: Resultsmentioning

confidence: 99%

Transposition of insertion sequence IS256Bsu1 in Bacillus subtilis 168 is strictly dependent on recA

et al. 2017

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“…Ax2 was cultured in HL5 medium (0.04% KH 2 PO 4 , 0.05% Na2HPO4, 0.7% yeast extract, 1.4% bacteriological peptone and 1% glucose, pH 6.5). The recA -strain was established as described in a previous report 5) . The null cells were maintained in HL5 containing 5 mg/l of blasticidin S (Funakoshi, Tokyo, Japan).…”

Section: Methodsmentioning

confidence: 99%

“…RT-PCR was performed using a One-Step RNA PCR Kit (Takara Shuzo, Kyoto, Japan). The primers and the reaction conditions were described in previous reports 5,9) . Reaction products were electrophoresed to analyze the signal intensity.…”

Section: Reverse Transcription-polymerase Chain Reaction (Rt-pcr)mentioning

confidence: 99%

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The recA-deficient Dictyostelium discoideum Forms Large Fruiting Bodies

2004

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The cellular slime mold Dictyostelium discoideum expresses a RecA homolog that is distributed in mitochondria. A gene disruption mutant is hypersensitive to DNA-damaging agents, indicating that RecA is required for the repair of mitochondrial DNA. We analyzed the process by which a multicellular structure of recA -cells is formed. Four hours after starvation, the internal glucose level of recA -cells (11.8±0.9 nmol/mg protein) was higher than that of wild-type cells (6.7±0.1 nmol/mg protein). The degree of cell-cell adhesion of recA -cells was greater than that of wild-type cells, while the migration speed of recA -cells (3.5±0.2 mm/min) was less than that of wild-type cells (4.3±0.3 mm/min). The increase in cell-cell adhesion and decrease in motility of recA -cells gave rise to the formation of large multicellular structures. The diameters of mounds formed by recA -and wildtype cells were 0.30±0.01 mm and 0.17±0.01 mm, respectively.

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“…As a result of EGT, eukaryotic RecA proteins are encoded in the nuclear genome, yet active inside organelles. These proteins are imported through the organellar membrane, after recognition by an N-terminus signalling transit peptide, which is cleaved in the organelle yielding the active protein [9][10][11].…”

Section: Introductionmentioning

confidence: 99%

Evolution of bacterial recombinase A ( recA ) in eukaryotes explained by addition of genomic data of key microbial lineages

et al. 2016

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Recombinase enzymes promote DNA repair by homologous recombination. The genes that encode them are ancestral to life, occurring in all known dominions: viruses, Eubacteria, Archaea and Eukaryota. Bacterial recombinases are also present in viruses and eukaryotic groups (supergroups), presumably via ancestral events of lateral gene transfer. The eukaryotic recA genes have two distinct origins (mitochondrial and plastidial), whose acquisition by eukaryotes was possible via primary (bacteria-eukaryote) and/or secondary (eukaryote-eukaryote) endosymbiotic gene transfers (EGTs). Here we present a comprehensive phylogenetic analysis of the recA genealogy, with substantially increased taxonomic sampling in the bacteria, viruses, eukaryotes and a special focus on the key eukaryotic supergroup Amoebozoa, earlier represented only by Dictyostelium. We demonstrate that several major eukaryotic lineages have lost the bacterial recombinases (including Opisthokonta and Excavata), whereas others have retained them (Amoebozoa, Archaeplastida and the SAR-supergroups). When absent, the bacterial recA homologues may have been lost entirely (secondary loss of canonical mitochondria) or replaced by other eukaryotic recombinases. RecA proteins have a transit peptide for organellar import, where they act. The reconstruction of the RecA phylogeny with its EGT events presented here retells the intertwined evolutionary history of eukaryotes and bacteria, while further illuminating the events of endosymbiosis in eukaryotes by expanding the collection of widespread genes that provide insight to this deep history.

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A homolog of Escherichia coli RecA in mitochondria of the cellular slime mold Dictyostelium discoideum

Cited by 7 publications

References 23 publications

Transposition of insertion sequence IS<i>256Bsu1</i> in <i>Bacillus subtilis</i> 168 is strictly dependent on <i>recA</i>

Transposition of insertion sequence IS<i>256Bsu1</i> in <i>Bacillus subtilis</i> 168 is strictly dependent on <i>recA</i>

The recA-deficient Dictyostelium discoideum Forms Large Fruiting Bodies

Evolution of bacterial recombinase A ( recA ) in eukaryotes explained by addition of genomic data of key microbial lineages

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