Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2006 Jan 8;34(1):175-84.
doi: 10.1093/nar/gkj401. Print 2006.

Oct-2 DNA binding transcription factor: functional consequences of phosphorylation and glycosylation

Ishtiaq Ahmad  1 , Daniel C Hoessli, Evelyne Walker-Nasir, Saleem M Rafik, Abdul R Shakoori, Nasir-ud-Din
Affiliations

Oct-2 DNA binding transcription factor: functional consequences of phosphorylation and glycosylation

Ishtiaq Ahmad et al. Nucleic Acids Res. .

Abstract

Phosphorylation and O-GlcNAc modification often induce conformational changes and allow the protein to specifically interact with other proteins. Interplay of phosphorylation and O-GlcNAc modification at the same conserved site may result in the protein undergoing functional switches. We describe that at conserved Ser/Thr residues of human Oct-2, alternative phosphorylation and O-GlcNAc modification (Yin Yang sites) can be predicted by the YinOYang1.2 method. We propose here that alternative phosphorylation and O-GlcNAc modification at Ser191 in the N-terminal region, Ser271 and 274 in the linker region of two POU sub-domains and Thr301 and Ser323 in the POUh subdomain are involved in the differential binding behavior of Oct-2 to the octamer DNA motif. This implies that phosphorylation or O-GlcNAc modification of the same amino acid may result in a different binding capacity of the modified protein. In the C-terminal domain, Ser371, 389 and 394 are additional Yin Yang sites that could be involved in the modulation of Oct-2 binding properties.

PubMed Disclaimer

Figures

Figure 1
Figure 1
Graphical representation of potential for O-GlcNAc modification in serine and threonine residues in the human Oct-2 sequence. Green vertical lines show the potential of S/T residues for O-GlcNAc modification and light blue horizontal wavy line shows threshold for modification potential.
Figure 2
Figure 2
(a) Potential for phosphate modification at serine and threonine residues in the human Oct-2 sequence and (b) sites with potential for both O-GlcNAc and phosphate, the Yin Yang sites with red asterisk at top.
Figure 3
Figure 3
Multiple alignments of five mammalian sequences (human, pig, dog, rat and mouse), one from fish (catfish) and one from Drosophila. The consensus sequence is highlighted by asterisk, conserved substitution by double dot and semiconserved substitution by single dot. Different sequences are ordered as in aligned results from CLUSTALW and the numbers in parenthesis show position of human Oct-2 sequence aligned with the others.
Figure 4
Figure 4
The phylogenetic tree generated by CLUSTALW with all sequences for mammalian, catfish and Drosophila Oct-2.
Figure 5
Figure 5
Sequence logos for different aligned regions of Oct-2. The conserved S/T residues with modification potential and with experimental evidence for modification in the region they are located are marked by a blue asterisk on the top of these residues. Whereas other conserved Ser residues are marked by red asterisk, which display either high or low potential as Yin Yang sites but lacking experimental evidence for modification in the region where they are located.
See this image and copyright information in PMC

References

    1. Pabo C.O., Sauer R.T. Protein–DNA recognition. Annu. Rev. Biochem. 1984;53:293–321. - PubMed
    1. Murre C., McCaw P.S., Baltimore D. A new DNA binding and dimerization motif in immunoglobulin enhancer binding, daughterless, MyoD, and myc proteins. Cell. 1989;56:777–783. - PubMed
    1. Gauss P., Krassa K.B., McPheeters D.S., Nelson M.A., Gold L. Zinc (II) and the single-stranded DNA binding protein of bacteriophage T4. Proc. Natl Acad. Sci. USA. 1987;84:8515–8519. - PMC - PubMed
    1. Landschultz W.H., Johnson P.F., McKnight S.L. The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins. Science. 1988;240:1759–1764. - PubMed
    1. Herr W., Sturm R.A., Clerc R.G., Corcoran L.M., Baltimore D., Sharp P.A., Ingraham H.A., Rosenfeld M.G., Finney M., Ruvkun G., Horvitz H.R. The POU domain: a large conserved region in the mammalian pit-1, Oct-1, Oct-2, and Caenorhabditis elegans unc-86 gene products. Genes Dev. 1988;2:1513–1516. - PubMed

Publication types