The ancient regulatory-protein family of WD-repeat proteins

  title={The ancient regulatory-protein family of WD-repeat proteins},
  author={Eva J. Neer and Carl J. Schmidt and Raman Nambudripad and Temple F. Smith},
WD proteins are made up of highly conserved repeating units usually ending with Trp-Asp (WD). They are found in all eukaryotes but not in prokaryotes. They regulate cellular functions, such as cell division, cell-fate determination, gene transcription, transmembrane signalling, mRNA modification and vesicle fusion. Here we define the common features of the repeating units, and criteria for grouping such proteins into functional subfamilies. 
GTP-binding proteins in plants
Current progress in the molecular characterization and functional analysis of plant genes encoding heterotrimeric and small GTPases is discussed and a systematic classification is proposed.
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Southern hybridization with probes designed for detection of WD-repeats coding sequences gave positive results in 21 streptomycete strains indicating that WD-repeats encoding genes are massively
The WD-repeat protein superfamily in Arabidopsis: conservation and divergence in structure and function
Most Arabidopsis WDR proteins are strongly conserved across eukaryotes, including those that have been found to play key roles in plant-specific processes, with diversity in function conferred at least in part by divergence in upstream signaling pathways, downstream regulatory targets and /or structure outside of the WDR regions.
A deduced Thermomonospora curvata protein containing serine/threonine protein kinase and WD-repeat domains
The gene pkwA coding for a typical WD-repeat protein was found in the chromosome of the bacterium Thermomonospora curvata CCM 3352, where it was found to be confined to eukaryotes.
Human Genome and Diseases:¶WD-repeat proteins: structure characteristics, biological function, and their involvement in human diseases
It is paramount to uncover the function of individual WD-repeat proteins, explore the protein interaction mechanism through WD- repeat domains and, ultimately, understand the complex biological processes and organisms themselves.
Wdr12, a mouse gene encoding a novel WD-Repeat Protein with a notchless-like amino-terminal domain.
The cloning of a mouse cDNA is reported, referred to as Wdr12, which encodes a novel WD-repeat protein of 423 amino acids, predicted to contain seven WD units and a nuclear localization signal located within a protruding peptide between the third and fourth WD domains.
Residues in the WD repeats of Tup1 required for interaction with alpha2
The yeast transcriptional repressor Tup1 contains seven WD repeats which interact with the DNA-binding protein alpha2, and mutations in Tup1 that disrupt this interaction are identified, suggesting that a similar structural interface is formed by WD repeat proteins that are used in both transcriptional regulation and signal transduction.
WD40 Repeat Proteins: Signalling Scaffold with Diverse Functions
The review summarizes the vast array of functions performed by different WD40 domain containing proteins, their domain organization and functional conservation during the course of evolution.


The WD‐40 repeat
A U3 snoRNP protein with homology to splicing factor PRP4 and G beta domains is required for ribosomal RNA processing.
In vivo depletion of SOF1 leads to impaired pre‐rRNA processing and inhibition of 18S rRNA production, sof1‐56 is a new component of the nucleolar rRNA processing machinery.
Human homologs of a Drosophila Enhancer of Split gene product define a novel family of nuclear proteins
Human cDNA clones encoding a family of proteins, designated TLE, that are homologous to the E(spl) m9/10 gene product, as well as a novel Notch–related protein are characterized.
Repetitive segmental structure of the transducin beta subunit: homology with the CDC4 gene and identification of related mRNAs.
  • H. Fong, J. Hurley, M. Simon
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1986
The results suggest that the mRNAs in retina are the processed products of a small number of closely related genes or of a single highly complex beta gene.
A G-protein beta-subunit is essential for Dictyostelium development.
It is proposed that G-protein heterotrimers are formed when this beta-subunit couples with each of the eight distinct G- protein alpha-subunits that are transiently expressed during development.
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