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Review
. 2000 Sep;20(17):6185-94.
doi: 10.1128/MCB.20.17.6185-6194.2000.

Class II transactivator: mastering the art of major histocompatibility complex expression

J A Harton  1 , J P Ting
Affiliations
Review

Class II transactivator: mastering the art of major histocompatibility complex expression

J A Harton et al. Mol Cell Biol. 2000 Sep.
No abstract available

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Figures

FIG. 1
FIG. 1
Organization of W, X, Y, and other motifs in the promoters of class II MHC and related genes. Genes coding for class II MHC and related proteins contain well conserved W, X, and Y boxes, the presence of which correlates with transcriptional regulation by CIITA.
FIG. 2
FIG. 2
Promoter organization for CIITA. The CIITA upstream region in humans contains four promoters (I to IV) with independent start sites and alternate first exons. Significant mRNA populations have only been observed for I, III, and IV in vivo. The 3′ splice site for the first exons of promoters I and III is upstream of the translation start site for promoter IV mRNA and thus adds seven amino acid residues (∗). The core 1,106 amino acids of CIITA may be encoded by as many as 17 exons.
FIG. 3
FIG. 3
Schematic representation of protein domain organization for CIITA. Numbering corresponds to the B-cell form of CIITA. The first 336 amino acids of CIITA contain both an acidic domain and the PST domain. Residues 336 to 1130 contain the GTP-binding, NLS, and LRR motifs. G1, G3, and G4 mark the positions of specific motifs required for GTP binding (see text).
FIG. 4
FIG. 4
The domain organization of CIITA is similar to those of other NBS- and LRR-containing proteins. CIITA is compared to two NBS- and LRR-containing proteins, mammalian Nod1 and the plant disease resistance protein RPM1 (see text). The N-terminal domains of these proteins are dissimilar. Tick marks, intervals of approximately 100 amino acids.
FIG. 5
FIG. 5
Multiple transcription factor contacts allow CIITA to function as a transcriptional scaffold and integrator. CIITA contacts components of the basal transcription machinery via its acidic domain. Interactions with RFX, RFXANK, CREB (X2BP), NF-YB, and NF-YC have been mapped. The region of CIITA required for each interaction is shown (see text). Domain markings for CIITA are the same as in Fig. 3. TBP, TATA-binding protein.
See this image and copyright information in PMC

References

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