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MYB (gene)

From Wikipedia, the free encyclopedia

Myb-like DNA-binding domain
Identifiers
SymbolMyb_DNA-binding
PfamPF00249
InterProIPR001005
PROSITEPDOC00037
CATH1irz
SCOP21irz / SCOPe / SUPFAM
CDDcd00167
Available protein structures:
PDB  IPR001005 PF00249 (ECOD; PDBsum)  
AlphaFold
MYB
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesMYB, Cmyb, c-myb, c-myb_CDS, efg, MYB proto-oncogene, transcription factor
External IDsOMIM: 189990; MGI: 97249; HomoloGene: 31311; GeneCards: MYB; OMA:MYB - orthologs
Orthologs
SpeciesHumanMouse
Entrez

4602

17863

Ensembl

ENSG00000118513

ENSMUSG00000019982

UniProt

P10242
Q708E1

P06876

RefSeq (mRNA)

NM_001198914
NM_010848
NM_033597

RefSeq (protein)

NP_001185843
NP_034978

Location (UCSC)Chr 6: 135.18 – 135.22 MbChr 10: 21 – 21.04 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Myb genes are part of a large gene family of transcription factors found in animals, plants, and fungi[5]. In humans, it includes Myb proto-oncogene like 1 and Myb-related protein B in addition to MYB proper.[6][7] Members of the extended SANT/Myb family also include the SANT domain and other similar all-helical homeobox-like domains.

Function

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Viral

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The Myb gene family is named after the eponymous gene in Avian myeloblastosis virus. The viral Myb (v-Myb, P01104) recognizes the sequence 5'-YAACKG-3'. It causes myeloblastosis (myeloid leukemia) in chickens.[8] Compared to the normal animal cellular Myb (c-myb), v-myb contains deletions in the C-terminal regulatory domain, leading to aberrant activation of other oncogenes.[9]

Animals

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Myb proto-oncogene protein is a member of the MYB (myeloblastosis) family of transcription factors. The protein contains three domains, an N-terminal DNA-binding domain, a central transcriptional activation domain and a C-terminal domain involved in transcriptional repression. It may play a role in cell cycle regulation. Like the viral version, this gene is an oncogene, and rearrangements of the gene (often involving deletion in the C-terminal domain) causes cancer.[9]

Plants

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MYB factors represent a family of proteins that include the conserved MYB DNA-binding domain. Plants contain a MYB-protein subfamily that is characterised by the R2R3-type MYB domain.[10]

In maize, phlobaphenes are synthesized in the flavonoids synthetic pathway[11] from polymerisation of flavan-4-ols[12][13] which encodes an R2R3 myb-like transcriptional activator[14] of the A1 gene encoding for the dihydroflavonol 4-reductase (reducing dihydroflavonols into flavan-4-ols)[15] while another gene (Suppressor of Pericarp Pigmentation 1 or SPP1) acts as a suppressor.[16] The maize P gene encodes a Myb homolog that recognizes the sequence CCWACC, in sharp contrast with the YAACGG bound by vertebrate Myb proteins.[17]

In sorghum, the corresponding yellow seed 1 gene (y1)[18] also encodes a R2R3 type of Myb domain protein that regulates the expression of chalcone synthase, chalcone isomerase and dihydroflavonol reductase genes required for the biosynthesis of 3-deoxyflavonoids.[19]

Ruby is a MYB transcriptional activator of genes that produce anthocyanin in citrus fruits. In most citrus varieties Ruby is non-functional, but in blood oranges it upregulates anthocyanin production to produce the characteristic red color of the fruit.[20]

See also

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References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000118513 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000019982 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Kurita G, Adachi KA, Uesaka K, Goshima G (February 2026). "Genetic switch between unicellularity and multicellularity in marine yeasts". Nature. 650 (8103): 909–919. doi:10.1038/s41586-025-09881-4. PMID 41501449.
  6. ^ Chen Y, Xu H, Liu J, Zhang C, Leutz A, Mo X (Jul 2007). "The c-Myb functions as a downstream target of PDGF-mediated survival signal in vascular smooth muscle cells". Biochemical and Biophysical Research Communications. 360 (2): 433–436. Bibcode:2007BBRC..360..433C. doi:10.1016/j.bbrc.2007.06.078. PMID 17599807.
  7. ^ "Entrez Gene: v-myb myeloblastosis viral oncogene homolog (avian)".
  8. ^ Klempnauer KH, Symonds G, Evan GI, Bishop JM (June 1984). "Subcellular localization of proteins encoded by oncogenes of avian myeloblastosis virus and avian leukemia virus E26 and by chicken c-myb gene". Cell. 37 (2): 537–547. doi:10.1016/0092-8674(84)90384-2. PMID 6327074. S2CID 46196167.
  9. ^ a b George OL, Ness SA (October 2014). "Situational awareness: regulation of the myb transcription factor in differentiation, the cell cycle and oncogenesis". Cancers. 6 (4): 2049–2071. doi:10.3390/cancers6042049. PMC 4276956. PMID 25279451.
  10. ^ Stracke R, Werber M, Weisshaar B (October 2001). "The R2R3-MYB gene family in Arabidopsis thaliana". Current Opinion in Plant Biology. 4 (5): 447–456. Bibcode:2001COPB....4..447S. doi:10.1016/s1369-5266(00)00199-0. PMID 11597504.
  11. ^ Himi E, Mares DJ, Yanagisawa A, Noda K (July 2002). "Effect of grain colour gene (R) on grain dormancy and sensitivity of the embryo to abscisic acid (ABA) in wheat". Journal of Experimental Botany. 53 (374): 1569–1574. doi:10.1093/jxb/erf005. PMID 12096095.
  12. ^ Winkel-Shirley B (June 2001). "Flavonoid biosynthesis. A colorful model for genetics, biochemistry, cell biology, and biotechnology". Plant Physiology. 126 (2): 485–493. doi:10.1104/pp.126.2.485. PMC 1540115. PMID 11402179.
  13. ^ Chopra S, Cocciolone SM, Bushman S, Sangar V, McMullen MD, Peterson T (March 2003). "The maize unstable factor for orange1 is a dominant epigenetic modifier of a tissue specifically silent allele of pericarp color1". Genetics. 163 (3): 1135–1146. doi:10.1093/genetics/163.3.1135. PMC 1462483. PMID 12663550.
  14. ^ Structural And Transcriptional Analysis Of The Complex P1-wr Cluster In Maize. Wolfgang Goettel, Joachim Messing. Plant & Animal Genomes XVI Conference Archived 2012-02-18 at the Wayback Machine
  15. ^ Dong X, Braun EL, Grotewold E (September 2001). "Functional conservation of plant secondary metabolic enzymes revealed by complementation of Arabidopsis flavonoid mutants with maize genes" (PDF). Plant Physiology. 127 (1): 46–57. doi:10.1104/pp.127.1.46. hdl:1811/48809. PMC 117961. PMID 11553733.
  16. ^ Lee EA, Harper V (2002). "Suppressor of Pericarp Pigmentation 1 (SPP1), a novel gene involved in phlobaphene accumulation in maize (Zea mays L.) pericarps". Maydica. 47 (1): 51–58. INIST 13772300
  17. ^ Grotewold E, Drummond BJ, Bowen B, Peterson T (1994). "The myb-homologous P gene controls phlobaphene pigmentation in maize floral organs by directly activating a flavonoid biosynthetic gene subset". Cell. 76 (3): 543–554. doi:10.1016/0092-8674(94)90117-1. PMID 8313474. S2CID 42197232.
  18. ^ Boddu J, Svabek C, Ibraheem F, Jones AD, Chopra S (2005). "Characterization of a deletion allele of a sorghum Myb gene yellow seedl showing loss of 3-deoxyflavonoids". Plant Science. 169 (3): 542–552. Bibcode:2005PlnSc.169..542B. doi:10.1016/j.plantsci.2005.05.007. INIST 16983977
  19. ^ Boddu J, Jiang C, Sangar V, Olson T, Peterson T, Chopra S (January 2006). "Comparative structural and functional characterization of sorghum and maize duplications containing orthologous myb transcription regulators of 3-deoxyflavonoid biosynthesis". Plant Molecular Biology. 60 (2): 185–199. Bibcode:2006PMolB..60..185B. doi:10.1007/s11103-005-3568-1. PMID 16429259. S2CID 23841582.
  20. ^ Butelli E, Licciardello C, Zhang Y, Liu J, Mackay S, Bailey P, et al. (2012). "Retrotransposons control fruit-specific, cold-dependent accumulation of anthocyanins in blood oranges". The Plant Cell. 24 (3): 1242–1255. Bibcode:2012PlanC..24.1242B. doi:10.1105/tpc.111.095232. PMC 3336134. PMID 22427337.

Further reading

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This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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