MYB (gene)

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V-myb avian myeloblastosis viral oncogene homolog
Protein MYB PDB 1guu.png
PDB rendering based on 1guu.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols MYB ; Cmyb; c-myb; c-myb_CDS; efg
External IDs OMIM189990 MGI97249 HomoloGene31311 GeneCards: MYB Gene
RNA expression pattern
PBB GE MYB 204798 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 4602 17863
Ensembl ENSG00000118513 ENSMUSG00000019982
UniProt P10242 P06876
RefSeq (mRNA) NM_001130172 NM_001198914
RefSeq (protein) NP_001123644 NP_001185843
Location (UCSC) Chr 6:
135.5 – 135.54 Mb
Chr 10:
21.12 – 21.16 Mb
PubMed search [1] [2]

Myb proto-oncogene protein also known as transcriptional activator Myb is a protein that in humans is encoded by the MYB gene.[1][2]

Function[edit]

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. This protein plays an essential role in the regulation of hematopoiesis and may play a role in tumorigenesis, including the regulation of miR-155 in B-cells.[3]

Plant orthologs[edit]

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.[4]

In maize, phlobaphenes are synthesized in the flavonoids synthetic pathway[5] from polymerisation of flavan-4-ols[6][7] which encodes an R2R3 myb-like transcriptional activator[8] of the A1 gene encoding for the dihydroflavonol 4-reductase (reducing dihydroflavonols into flavan-4-ols)[9] while another gene (Suppressor of Pericarp Pigmentation 1 or SPP1) acts as a suppressor.[10] The maize P gene encodes a Myb homolog that recognizes the sequence CCT/AACC, in sharp contrast with the C/TAACGG bound by vertebrate Myb proteins.[11]

In sorghum, the corresponding yellow seed 1 gene (y1)[12] 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.[13]

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. [14]

References[edit]

  1. ^ 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". Biochem Biophys Res Commun 360 (2): 433–6. doi:10.1016/j.bbrc.2007.06.078. PMID 17599807. 
  2. ^ "Entrez Gene: v-myb myeloblastosis viral oncogene homolog (avian)". 
  3. ^ Vargova K, Curik N, Burda P, Basova P, Kulvait V, Pospisil V, Savvulidi F, Kokavec J, Necas E, Berkova A, Obrtlikova P, Karban J, Mraz M, Pospisilova S, Mayer J, Trneny M, Zavadil J, Stopka T (April 2011). "MYB transcriptionally regulates the miR-155 host gene in chronic lymphocytic leukemia". Blood 117 (14): 3816–25. doi:10.1182/blood-2010-05-285064. PMID 21296997. 
  4. ^ Stracke R, Werber M, Weisshaar B (October 2001). "The R2R3-MYB gene family in Arabidopsis thaliana". Curr. Opin. Plant Biol. 4 (5): 447–56. doi:10.1016/s1369-5266(00)00199-0. PMID 11597504. 
  5. ^ 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". J. Exp. Bot. 53 (374): 1569–74. doi:10.1093/jxb/erf005. PMID 12096095. 
  6. ^ Winkel-Shirley B (June 2001). "Flavonoid biosynthesis. A colorful model for genetics, biochemistry, cell biology, and biotechnology". Plant Physiol. 126 (2): 485–93. doi:10.1104/pp.126.2.485. PMC 1540115. PMID 11402179. 
  7. ^ 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): 1135–46. PMC 1462483. PMID 12663550. 
  8. ^ Structural And Transcriptional Analysis Of The Complex P1-wr Cluster In Maize. Wolfgang Goettel, Joachim Messing. Plant & Animal Genomes XVI Conference
  9. ^ 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". Plant Physiol. 127 (1): 46–57. doi:10.1104/pp.127.1.46. PMC 117961. PMID 11553733. 
  10. ^ 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
  11. ^ The myb-homologous P gene controls phlobaphene pigmentation in maize floral organs by directly activating a flavonoid biosynthetic gene subset. Erich Grotewold, Bruce J. Drummond, Ben Bowen and Thomas Peterson, Cell, 11 February 199, Volume 76, Issue 3, pages 543-554, doi:10.1016/0092-8674(94)90117-1 PMID 8313474
  12. ^ 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. doi:10.1016/j.plantsci.2005.05.007.  INIST:16983977
  13. ^ 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 Mol. Biol. 60 (2): 185–99. doi:10.1007/s11103-005-3568-1. PMID 16429259. 
  14. ^ Butelli E, Licciardello C, Zhang Y, Liu J, Mackay S, Bailey P, Reforgiato-Recupero G, Martin C (2012). "Retrotransposons control fruit-specific, cold-dependent accumulation of anthocyanins in blood oranges". Plant Cell 24 (3): 1242–55. doi:10.1105/tpc.111.095232. PMC 3336134. PMID 22427337. 

Further reading[edit]

External links[edit]

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