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Published byKamilla Børresen Modified over 6 years ago
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Purposes: To demonstrate the tendency of proteins to become longer with increase of organism complexity To study domain architecture of proteins and to date different domains
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Homologous proteins Orthologs Paralogs
Have evolved by vertical descent from a common ancestor and are presumed to have complete structural and functional correspondence Arise by duplication and domain shuffling within a genome and hence may have divergent functions New function We are interested in proteins that have changed their domain content, but preserved the same function
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Human HRX protein PHD zf-CXXC SET FYRN FYRC BROMO
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Plant PHD SET BROMO zf-CXXC FYRC FYRN zf-C4 RRM PostSET HMG PWWP TUDOR
gi| |gb|AAK |AF401284_1 trithorax 3 [Arabidopsis thaliana] (330 letters) gi| |ref|NP_ | putative protein [Arabidopsis thaliana] (902 letters) gi| |gb|AAF |AC009999_10 Contains similarity to MLL proteinfrom Fugu rubripes gb|AF036382, and contains a PWWP PF|00855 and a SET PF|00856 domain. [Arabidopsis thaliana] (1193 letters) gi| |ref|NP_ | putative SET-domain transcriptional regulator [Arabidopsis thaliana] (186 letters) gi| |ref|NP_ | putative protein [Arabidopsis thaliana] (1040 letters) gi| |gb|AAL | trithorax 4 [Arabidopsis thaliana] (285 letters) gi| |ref|NP_ | putative protein [Arabidopsis thaliana] (1421 letters) gi| |ref|NP_ | unknown protein [Arabidopsis thaliana] (764 letters)
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Yeast Worm PHD SET BROMO zf-CXXC FYRC FYRN zf-C4 RRM PostSET HMG PWWP
TUDOR gi| |pir||T41282 probable transcription silencing protein - fission yeast (Schizosaccharomyces pombe) (920 letters) gi| |ref|NP_ | Gene has a 'SET' or 'TROMO' domain at its carboxyterminus like the trithorax gene family from human and Drosophila with postulated function in chromatin-mediated gene regulation.; Set1p [Saccharomyces cerevisiae] (1080 letters) Yeast Worm gi| |ref|NP_ | C26E6.9a.p [Caenorhabditis elegans] (1507 letters) + gi| |ref|NP_ | C26E6.9b.p [Caenorhabditis elegans] (739 letters) gi| |ref|NP_ | PHD-finger. (2 domains), SET domain [Caenorhabditis elegans] (2561 letters)
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Fly PHD SET BROMO zf-CXXC FYRC FYRN zf-C4 RRM PostSET HMG PWWP TUDOR
gi| |gb|AAL | GM10003p [Drosophila melanogaster] (421 letters) gi| |pir||T12687 ALR protein homolog - fruit fly (Drosophila melanogaster) (2422 letters) gi| |gb|AAF | CG17396 gene product [Drosophila melanogaster] (177 letters) gi|469801|emb|CAA | predicted trithorax protein [Drosophila melanogaster] (3358 letters) gi| |gb|AAF | CG5591 gene product [Drosophila melanogaster] (630 letters) gi| |gb|AAK | LD39445p [Drosophila melanogaster] (700 letters) gi| |sp|Q24742|TRX_DROVI Trithorax protein (3828 letters)
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Human PHD SET BROMO zf-CXXC FYRC FYRN zf-C4 RRM PostSET HMG PWWP TUDOR
gi| |sp|Q03164|HRX_HUMAN Zinc finger protein HRX (ALL-1) (Trithorax-like protein) (3969 letters) gi| |gb|AAD | myeloid/lymphoid leukemia 2 [Homo sapiens] (1010 letters) gi| |dbj|BAA | KIAA0304 protein [Homo sapiens] (1900 letters) gi| |gb|AAH |AAH09337 Similar to KIAA0304 gene product [Homo sapiens] (798 letters) gi| |gb|AAH |AAH07353 Similar to KIAA0304 gene product [Homo sapiens] (140 letters) gi| |gb|AAD |AF105280_1 myeloid/lymphoid leukemia 2 [Homo sapiens] (140 letters)
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Human - continued PHD SET BROMO zf-CXXC FYRC FYRN zf-C4 RRM PostSET
HMG PWWP TUDOR Human - continued gi| |ref|NP_ | mixed-lineage leukemia 2; ALL1-related gene [Homo sapiens] (5262 letters) gi| |pir||T03455 ALR protein - human (4957 letters) gi| |dbj|BAA | KIAA0339 protein [Homo sapiens] (1709 letters) gi| |ref|XP_ | KIAA1076 protein [Homo sapiens] (772 letters) gi| |ref|NP_ | mixed-lineage leukemia 3; ALR-like protein [Homo sapiens] (4025 letters) gi| |dbj|BAB | unnamed protein product [Homo sapiens] (452 letters)
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940Ma 1087Ma 1508Ma Protista PHD SET BROMO zf-CXXC FYRC FYRN zf-C4 RRM
PostSET HMG PWWP TUDOR Vertebrates Homo sapiens 940Ma Arthropods Drosophyla melanogaster Drosophyla virilis 1087Ma Nematodes Caenorhabditis elegans Fungi Schizosaccharomyces pombe Saccharomyces cerevisiae 1508Ma Protista Plants Arabidopsis thaliana
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Conclusion: Elongation of proteins within interspecific trx family is correlated with organism complexity Proteins elongate following domain duplication, shuffling and accretion
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