mfd

mfd
168

transcription-repair coupling factor, eliminates genetic damage from transcriptionally active genes during sporulation, required for increased mutagenesis of lagging strand genes

Locus
BSU_00550
Molecular weight
133.59 kDa
Isoelectric point
5.37
Protein length
1177 aaSequenceBlast
Gene length
3534 bpSequenceBlast
Function
promotes strand-specific DNA repair by displacing
Product
transcription-repair coupling factor
Essential
no
E.C.
3.6.4.-
Synonyms
mfd
Outlinks
BsubCyc SubtiList UniProt STRING Genoscapist PaperBLAST

Genomic Context

Categories containing this gene/protein

List of homologs in different organisms, belongs to COG1197 (Galperin et al., 2021)

This gene is a member of the following regulons

Gene
Coordinates
60,430  63,963
Phenotypes of a mutant
in an mfd knock-out, the cell's ability to accumulate adaptive mutations in stationary phase is depressed PubMed
strongly reduced stationary phase mutagenesis PubMed
reduced formation of rpsB or rpsE suppressor mutants after mitomycin treatment PubMed
increased UV-induced mutagenesis via PolY1/ PolY2-mediated translesion synthesis PubMed
the mutation suppresses the mucoid phenotype of ''motA or motB'' mutants PubMed
sensitive to blue light-induced DNA damage PubMed
sensitive to oxidative stress PubMed
suppression of lethality of pcrA inactivation PubMed
The protein
Catalyzed reaction/ biological activity
promotes strand-specific DNA repair by displacing RNA polymerase stalled at a nucleotide lesion and directing the (A)BC excinuclease to RNA damage site
is required for roadblock transcription repression by transcription factors with binding sites downstream of the promoter (as for CcpA PubMed and CodY PubMed)
required for the processing of genetic damage during sporulation PubMed
required for repair of DNA lesions during growth PubMed
promotes error-prone DNA repair during stress to promote genetic diversity PubMed
couples transcription to nucleotide excision repair (NER) to eliminate DNA distorting lesions during sporulation PubMed
Protein family
N-terminal part: UvrB family (with UvrB, according to UniProt)
C-terminal part: helicase family (according to UniProt)
Domains
Helicase ATP-binding domain (aa 638-799) (according to UniProt)
Helicase C-terminal domain (aa 820-974) (according to UniProt)
Structure
2EYQ (PDB) (Mfd from E. coli) PubMed
3MLQ (PDB) (RNA polymerase interacting domain of Thermus thermophilus Mfd with the Thermus aquaticus RpoB beta1 domain) PubMed
P37474 (AlphaFold)
Paralogous protein(s)
RecU, RecG
Localization
cytoplasm (according to UniProt)
Expression and Regulation
Operons
Genes
fin-mfd-spoVT
Description
PubMed
Expression
expression is heterogeneous PubMed
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fin→spoVT

2025-03-17 13:30:11

Jstuelk

141

24843A2E745DD5C1C92792486D51FED74A35A094

F1FF2D64FF9C8F7A797DEED100A7732A06763FB4

Biological materials
Mutant
GP3519 (Δmfd::kan), available in Jörg Stülke's lab
GP1167 (Δmfd::ermC), available in Jörg Stülke's lab PubMed
BKE00550 (''mfd::erm'', available in the BGSC, in Fabian Commichau's, and in Jörg Stülke's labs) PubMed
BKE00550 (mfd::erm  trpC2) available at BGSC,  PubMed, upstream reverse: _UP1_CATATGGCCCCTCCTCTCTG,  downstream forward: _UP4_TAAATTTTGTTACTCTCTGG
BKK00550 (mfd::kan  trpC2) available at BGSC,  PubMed, upstream reverse: _UP1_CATATGGCCCCTCCTCTCTG,  downstream forward: _UP4_TAAATTTTGTTACTCTCTGG
Two-hybrid system
B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Fabian Commichau's lab
GFP fusion
GP1510 (spc, based on pGP1870, pGP1389-derivative ), available in Jörg Stülke's lab
References
Reviews
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Original Publications
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AD1F39823ABCE2A222259B879513752942C59590

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Time of last update: 2025-04-02 08:30:30

Author of last update: Jstuelk