Squamosa promoter binding protein

The SQUAMOSA promoter binding protein-like (SBP or SPL) family of transcription factors are defined by a plant-specific DNA-binding domain. The founding member of the family was identified based on its specific in vitro binding to the promoter of the snapdragon SQUAMOSA gene.[1] SBP proteins are thought to be transcriptional activators.

SBP
Solution structure of the DNA-binding domain of Squamosa promoter binding protein-like 4
Identifiers
SymbolSBP
PfamPF03110
InterProIPR004333
PROSITEPDOC00798
SCOP22lao / SCOPe / SUPFAM
TCDB3.A.1
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Function

SPB proteins have roles in leaf development, vegetative phase change, flower and fruit development, plant architecture, sporogenesis, Gibberelic acid signaling and toxin response.[2]

Structure

The domain contains 10 conserved cysteine and histidine residues that probably are zinc ligands. The SBP domain is a highly conserved DNA-binding domain. It is approximately 80 amino acids in length and contains a zinc finger motif with two zinc-binding sites: Cys-Cys-His-Cys and Cys-Cys-Cys-His. It has a three-stranded antiparallel beta-sheet.[3]

References
  1. Klein J, Saedler H, Huijser P (January 1996). "A new family of DNA binding proteins includes putative transcriptional regulators of the Antirrhinum majus floral meristem identity gene SQUAMOSA". Mol. Gen. Genet. 250 (1): 7–16. doi:10.1007/bf02191820. PMID 8569690. S2CID 20915344.
  2. Chen X, Zhang Z, Liu D, Zhang K, Li A, Mao L (2010). "SQUAMOSA promoter-binding protein-like transcription factors: star players for plant growth and development". Journal of Integrative Plant Biology. 52 (11): 946–51. doi:10.1111/j.1744-7909.2010.00987.x. PMID 20977652.
  3. Yamasaki K, Kigawa T, Inoue M, Tateno M, Yamasaki T, Yabuki T, et al. (2004). "A novel zinc-binding motif revealed by solution structures of DNA-binding domains of Arabidopsis SBP-family transcription factors". J Mol Biol. 337 (1): 49–63. doi:10.1016/j.jmb.2004.01.015. PMID 15001351.
This article incorporates text from the public domain Pfam and InterPro: IPR004333


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