Genomic Evolution of the Distal Mhc Class I Region on Mouse Chr 17

Yoshino, Masayasu; Xiao, Hong; Jones, Elsy P.; Kumánovics, Attila; Amadou, Claire; Lindahl, Kirsten Fischer

doi:10.1111/j.1601-5223.1997.00141.x

Cited by 12 publications

(2 citation statements)

References 56 publications

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“…Taking the previously established region of conserved synteny between human and mouse (Yoshino et al 1997) into account, we have divided the human MHClinked OR cluster into two subclusters: the MHC-linked major OR cluster (562 kb between positions 105 and 667 kb in Fig. 1) and the MHC-linked minor OR cluster (between HFE and RFP).…”

Section: Gene Organization and Genomic Environmentmentioning

confidence: 99%

Characterization of Clustered MHC-Linked Olfactory Receptor Genes in Human and Mouse

Younger¹,

Amadou²,

Bethel³

et al. 2001

Genome Res.

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Olfactory receptor (OR) loci frequently cluster and are present on most human chromosomes. They are members of the seven transmembrane receptor (7-TM) superfamily and, as such, are part of one of the largest mammalian multigene families, with an estimated copy number of up to 1000 ORs per haploid genome. As their name implies, ORs are known to be involved in the perception of odors and possibly also in other, nonolfaction-related, functions. Here, we report the characterization of ORs that are part of the MHC-linked OR clusters in human and mouse (partial sequence only). These clusters are of particular interest because of their possible involvement in olfaction-driven mate selection. In total, we describe 50 novel OR loci (36 human, 14 murine), making the human MHC-linked cluster the largest sequenced OR cluster in any organism so far. Comparative and phylogenetic analyses confirm the cluster to be MHC-linked but divergent in both species and allow the identification of at least one ortholog that will be useful for future regulatory and functional studies. Quantitative feature analysis shows clear evidence of duplications of blocks of OR genes and reveals the entire cluster to have a genomic environment that is very different from its neighboring regions. Based on in silico transcript analysis, we also present evidence of extensive long-distance splicing in the 5′-untranslated regions and, for the first time, of alternative splicing within the single coding exon of ORs. Taken together with our previous finding that ORs are also polymorphic, the presented data indicate that the expression, function, and evolution of these interesting genes might be more complex than previously thought.[The sequence data described in this paper have been submitted to the EMBL nucleotide data library under accession nos.Z84475, Z98744, Z98745, AL021807, AL021808, AL022723, AL022727,AL031893, AL035402, AL035542, AL050328, AL050339, AL078630, AL096770,AL121944, AL133160, and AL133267.]

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Section: Gene Organization and Genomic Environmentmentioning

confidence: 99%

Characterization of Clustered MHC-Linked Olfactory Receptor Genes in Human and Mouse

Younger¹,

Amadou²,

Bethel³

et al. 2001

Genome Res.

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“…MHC class II molecules are composed of the a and b chains, which are type I transmembrane glycoproteins and associate through noncovalent interactions (34). MHC class I molecules are encoded by the K and D regions on mouse chromosome 17 and by the A, B, and C loci on human chromosome 6 (100,229,318). MHC class I molecules contain a 45-kDa heavy chain that associates through noncovalent interactions with the 12-kDa b 2 m light chain.…”

Section: Elements Of the Immune System And Their Functionsmentioning

confidence: 99%

Molecular Mechanisms of MHC Class I-Antigen Processing: Redox Considerations

Kim

Kang

Kim

et al. 2009

Antioxidants & Redox Signaling

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Major histocompatibility complex (MHC) class I molecules present antigenic peptides to the cell surface for screening by CD8(+) T cells. A number of ER-resident chaperones assist the assembly of peptides onto MHC class I molecules, a process that can be divided into several steps. Early folding of the MHC class I heavy chain is followed by its association with beta(2)-microglobulin (beta(2)m). The MHC class I heavy chain-beta(2)m heterodimer is incorporated into the peptide-loading complex, leading to peptide loading, release of the peptide-filled MHC class I molecules from the peptide-loading complex, and exit of the complete MHC class I complex from the ER. Because proper antigen presentation is vital for normal immune responses, the assembly of MHC class I molecules requires tight regulation. Emerging evidence indicates that thiol-based redox regulation plays critical roles in MHC class I-restricted antigen processing and presentation, establishing an unexpected link between redox biology and antigen processing. We review the influences of redox regulation on antigen processing and presentation. Because redox signaling pathways are a rich source of validated drug targets, newly discovered redox biology-mediated mechanisms of antigen processing may facilitate the development of more selective and therapeutic drugs or vaccines against immune diseases.

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