MSH6

MSH6
Dostupne strukture PDB Pretraga ortologa: PDBe RCSB Spisak PDB ID kodova 2O8F, 2GFU, 2O8B, 2O8C, 2O8D, 2O8E
Identifikatori
Aliasi	MSH6
Vanjski ID-jevi	OMIM: 600678 MGI: 1343961 HomoloGene: 149 GeneCards: MSH6
Lokacija gena (čovjek) Hrom. Hromosom 2 (čovjek)[1] Bend 2p16.3 Početak 47,695,530 bp[1] Kraj 47,810,063 bp[1]
Lokacija gena (miš) Hrom. Hromosom 17 (miš)[2] Bend 17 E4|17 57.87 cM Početak 88,282,490 bp[2] Kraj 88,298,320 bp[2]
Obrazac RNK ekspresije Više referentnih podataka o ekspresiji
Ontologija gena Molekularna funkcija • nucleotide binding • vezivanje sa DNK • protein homodimerization activity • mismatched DNA binding • ADP binding • chromatin binding • oxidized purine DNA binding • methylated histone binding • oštećeno vezivanje sa DNK • ATPase activity • GO:0001948, GO:0016582 vezivanje za proteine • single thymine insertion binding • four-way junction DNA binding • MutLalpha complex binding • double-stranded DNA binding • ATP binding • magnesium ion binding • single guanine insertion binding • guanine/thymine mispair binding • ATP-dependent activity, acting on DNA • vezivanje enzima Ćelijska komponenta • Golđijev aparat • intracellular membrane-bounded organelle • MutSalpha complex • nukleoplazma • hromosom • jedro • citosol • mismatch repair complex Biološki proces • determination of adult lifespan • cellular response to DNA damage stimulus • positive regulation of isotype switching • intrinsic apoptotic signaling pathway • maintenance of DNA repeat elements • positive regulation of helicase activity • somatic recombination of immunoglobulin gene segments • negative regulation of DNA recombination • Popravak neusklađenosti DNK • GO:0022415 viral process • GO:0100026 Popravka DNK • meiotic mismatch repair • intrinsic apoptotic signaling pathway in response to DNA damage • response to UV • somatic hypermutation of immunoglobulin genes • Promjena imunoglobulinske klase • pyrimidine dimer repair • mitotic G2 DNA damage checkpoint signaling • negative regulation of DNA endoreduplication • interstrand cross-link repair • replication fork arrest Izvori:Amigo / QuickGO
Ortolozi
Vrste	Čovjek	Miš
Entrez	2956	17688
Ensembl	ENSG00000116062	ENSMUSG00000005370
UniProt	P52701	P54276
RefSeq (mRNK)	NM_000179 NM_001281492 NM_001281493 NM_001281494	NM_010830
RefSeq (bjelančevina)	NP_000170 NP_001268421 NP_001268422 NP_001268423	NP_034960
Lokacija (UCSC)	Chr 2: 47.7 – 47.81 Mb	Chr 17: 88.28 – 88.3 Mb
PubMed pretraga	[3]	[4]
Wikipodaci
Pogledaj/uredi – čovjek Pogledaj/uredi – miš

MSH6 ili mutS homolog 6 jest gen koji se kod ljudi nalazi na hromosomu 2. To je gen koji kodira protein Msh6 za popravak neusklađenosti DNK u pupajućem kvascu Saccharomyces cerevisiae. To je homolog ljudskog "G/T vezujućeg proteina" (GTBP) koji se također naziva p160 ili hMSH6 (ljudski MSH6). Protein MSH6 je član mutatora S (MutS), porodice proteina koji su uključeni u popravku oštećenja DNK.

Defekti u hMSH6 su povezani sa atipskim nasljednim nepolipoznim kolorektumskim karcinomom koji ne ispunjava Amsterdamske kriterije za HNPCC. Mutacije hMSH6 su takođe povezane sa karcinomom endometrija i razvojem karcinoma endometrijuma.

Otkriće

MSH6 je prvi put identificiran u kvascu S. cerevisiae zbog svoje homologije sa MSH2. Identifikacija ljudsog gena GTBP i naknadna dostupnost aminokiselinske sekvence pokazala je da su MSH6 kvasca i ljudski GTBP više povezani jedni s drugima nego bilo koji drugi MutS homolog, sa 26,6% aminokiselinskog identiteta.^[5] Tako je GTBP dobio ime ljudski MSH6 ili hMSH6.

Amiokiselininska sekvenca

Dužina polipeptidnog lanca je 1.360 aminokiselina, a molkekulska iežina 152.786 Da.^[6]

• C: Cistein
• D: Asparaginska kiselina
• E: Glutaminska kiselina
• F: Fenilalanin
• G: Glicin
• H: Histidin
• I: Izoleucin
• K: Lizin
• L: Leucin
• M: Metionin
• N: Asparagin
• P: Prolin
• Q: Glutamin
• R: Arginin
• S: Serin
• T: Treonin
• V: Valin
• W: Triptofan
• Y: Tirozin

10		20		30		40		50
MSRQSTLYSF		FPKSPALSDA		NKASARASRE		GGRAAAAPGA		SPSPGGDAAW
SEAGPGPRPL		ARSASPPKAK		NLNGGLRRSV		APAAPTSCDF		SPGDLVWAKM
EGYPWWPCLV		YNHPFDGTFI		REKGKSVRVH		VQFFDDSPTR		GWVSKRLLKP
YTGSKSKEAQ		KGGHFYSAKP		EILRAMQRAD		EALNKDKIKR		LELAVCDEPS
EPEEEEEMEV		GTTYVTDKSE		EDNEIESEEE		VQPKTQGSRR		SSRQIKKRRV
ISDSESDIGG		SDVEFKPDTK		EEGSSDEISS		GVGDSESEGL		NSPVKVARKR
KRMVTGNGSL		KRKSSRKETP		SATKQATSIS		SETKNTLRAF		SAPQNSESQA
HVSGGGDDSS		RPTVWYHETL		EWLKEEKRRD		EHRRRPDHPD		FDASTLYVPE
DFLNSCTPGM		RKWWQIKSQN		FDLVICYKVG		KFYELYHMDA		LIGVSELGLV
FMKGNWAHSG		FPEIAFGRYS		DSLVQKGYKV		ARVEQTETPE		MMEARCRKMA
HISKYDRVVR		REICRIITKG		TQTYSVLEGD		PSENYSKYLL		SLKEKEEDSS
GHTRAYGVCF		VDTSLGKFFI		GQFSDDRHCS		RFRTLVAHYP		PVQVLFEKGN
LSKETKTILK		SSLSCSLQEG		LIPGSQFWDA		SKTLRTLLEE		EYFREKLSDG
IGVMLPQVLK		GMTSESDSIG		LTPGEKSELA		LSALGGCVFY		LKKCLIDQEL
LSMANFEEYI		PLDSDTVSTT		RSGAIFTKAY		QRMVLDAVTL		NNLEIFLNGT
NGSTEGTLLE		RVDTCHTPFG		KRLLKQWLCA		PLCNHYAIND		RLDAIEDLMV
VPDKISEVVE		LLKKLPDLER		LLSKIHNVGS		PLKSQNHPDS		RAIMYEETTY
SKKKIIDFLS		ALEGFKVMCK		IIGIMEEVAD		GFKSKILKQV		ISLQTKNPEG
RFPDLTVELN		RWDTAFDHEK		ARKTGLITPK		AGFDSDYDQA		LADIRENEQS
LLEYLEKQRN		RIGCRTIVYW		GIGRNRYQLE		IPENFTTRNL		PEEYELKSTK
KGCKRYWTKT		IEKKLANLIN		AEERRDVSLK		DCMRRLFYNF		DKNYKDWQSA
VECIAVLDVL		LCLANYSRGG		DGPMCRPVIL		LPEDTPPFLE		LKGSRHPCIT
KTFFGDDFIP		NDILIGCEEE		EQENGKAYCV		LVTGPNMGGK		STLMRQAGLL
AVMAQMGCYV		PAEVCRLTPI		DRVFTRLGAS		DRIMSGESTF		FVELSETASI
LMHATAHSLV		LVDELGRGTA		TFDGTAIANA		VVKELAETIK		CRTLFSTHYH
SLVEDYSQNV		AVRLGHMACM		VENECEDPSQ		ETITFLYKFI		KGACPKSYGF
NAARLANLPE		EVIQKGHRKA		REFEKMNQSL		RLFREVCLAS		ERSTVDAEAV
HKLLTLIKEL

Struktura

U ljudskom genomu, hMSH6 nalazi se na hromozomu 2. Sadrži strukturni motiv koji vezuje Walker-A/B adeninski nukleotid, što je najkonzerviranija sekvenca pronađena u svim MutS homolozima.^[7] Kao i kod drugih MutS homologa, hMSH6 ima unutrašnju aktivnost ATPaze. Funkcionira isključivo kada je vezan za hMSH2 kao heterodimer, iako sam hMSH2 može funkcionirati kao homomultimer ili kao heterodimer s hMSH3.^[8]

Funkcija

Značaj popravke neusklađenosti

Nepodudarnosti se obično javljaju kao rezultat grešaka u replikaciji DNK, genetičke rekombinacije ili drugih hemijskih i fizičkih faktora.^[9] Prepoznavanje tih neusklađenosti i njihovo popravljanje izuzetno je važno za ćelije, jer neuspjeh u tome rezultira nestabilnošću mikrosatelita, povećanom stopom spontanih mutacija (fenotip mutatora) i osjetljivošću na HNPCC..^[7][10] hMSH6 se kombinuje sa hMSH2 i formira aktivni proteinski kompleks, hMutS alfa, koji se također naziva i hMSH2-hMSH6.

Prepoznavanje neusklađenosti

Prepoznavanje neusklađenosti putem ovog kompleksa regulirano je transformacijom ADP → ATP, što pruža dokaz da hMutS alfa kompleks funkcionira kao molekulni prekidač.^[11] U normalnoj DNK, adenin (A) se vezuje za timin (T), a citozin (C) se vezuje za guanin (G). Ponekad će doći do neusklađenosti u kojoj će se T povezati sa G, što se naziva G/T neusklađenost. Kada se prepozna G/T neusklađenost, hMutS alfa kompleks se veže i razmjenjuje ADP za ATP.^[10] Razmjena ADP → ATP uzrokuje konformacijsku promjenu za pretvaranje hMutS alfa u kliznu stezaljku koja može difundirati duž DNK kičme.^[10] ATP inducira oslobađanje kompleksa iz DNK i omogućava hMutS alfa da se disocira duž DNK kao klizna stezaljka. Ova transformacija pomaže u pokretanju nizvodnih događaja za popravku oštećene DNK.^[10]

Kancer

Iako mutacije u hMSH2 uzrokuju jak opći fenotip mutatora, mutacije u hMSH6 uzrokuju samo skroman muttorski fenotip.^[5] Na nivou gena, otkriveno je da mutacije uzrokuju prvenstveno mutacije supstitucije na jednoj bazi, što sugerira da uloga hMSH6 prvenstveno je za ispravljanje mutacija supstitucije jedne baze i u manjoj mjeri mutacija insercije/delecije jedne baze.^[5]

Mutacije u genu hMSH6 uzrokuju da protein bude nefunkcionalan ili samo djelomično aktivan, čime se smanjuje njegova sposobnost popravljanja grešaka u DNK. Gubitak funkcije MSH6 rezultira nestabilnošću kod ponavljanja mononukleotida.^[5] HNPCC je najčešće uzrokovan mutacijama u hMSH2 i hMLH1, ali mutacije u hMSH6 povezane su s atipskim oblikom HNPCC.^[12] Čini se da je penetrantnost kolorektumskog karcinoma niža u ovim mutacijama, što znači da je nizak udio nositelja mutacije hMSH6 prisutan sa bolešću. Rak endometrija, s druge strane, čini se važnijom kliničkom manifestacijom za žene nositeljice mutacije. Početak raka endometrija, kao i raka debelog crijeva u porodicama sa hMSH6 mutacijama je oko 50 godina. Ovo je odgođeno u poređenju sa pojavom tumora povezanih s hMSH2 u dobi od 44 godine.^[12]

Epigenetička kontrola MSH6 kod kancera

Dvije mikroRNK, miR21 i miR-155, ciljaju gene hMSH6 i hMSH2 za popravak DNK neusklađenosti (MMR), da uzrokuju smanjenu ekspresiju njihovih proteina.^[13][14] Ako je jedna ili druga od ove dvije mikroRNK pretjerano eksprimirana, proteini hMSH2 i hMSH6 su nedovoljno eksprimirani, što rezultira smanjenom popravkom neusklađenosti DNK i povećanom nestabilnošću mikrosatelita.

Jedna od ovih mikroRNK, miR21, regulirana je epigenetički metilacijskoh stanja CpG-ostrva u jednj ili drugoj od svoje dvije promotorske regije.^[15] Hipometilacija njegovog promotorskog regionapovezana je se povećanom ekspresijom miRNK.^[16] Visoka ekspresija mikroRNK izaziva represiju tih ciljnih gena (vidi mikroRNK utišavanje gena). U 66% do 90% oslučajeva raka debelog crijeva, miR-21 je nadeksprimiran,^[13] a općenito mjereni nivoi hMSH2 opadaju (a hMSH6 je nestabilan bez hMSH2^[14]).

Kada je miR-155 bio povišen, hMSH2 je bio nedovoljno eksprimiran u 44% do 67% istih tkiva (a hMSH6 je vjerovatno i nedovoljno eksprimiran, a također je nestabilan u odsustvu hMSH2).^[14]

Interakcije

Pokazano je da MSH6 reagruje sa MSH2,^{[17][18][19][20][21]} PCNA^[22][23][24] i BRCA1.^[17][25]

Također pogledajte

• Reparacija DNK

Reference

1. GRCh38: Ensembl release 89: ENSG00000116062 - Ensembl, maj 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000005370 - Ensembl, maj 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Marsischky GT, et al. (1996). "Redundancy of Saccharomyces cerevisiae MSH3 and MSH6 in MSH2-dependent mismatch repair". Genes Dev. 10 (4): 407–20. doi:10.1101/gad.10.4.407. PMID 8600025.
6. "UniProt, P52701" (jezik: engleski). Pristupljeno 13. 11. 2021.
7. Fishel R, Kolodner RD (1995). "Identification of mismatch repair genes and their role in the development of cancer". Current Opinion in Genetics & Development. 5 (3): 382–95. doi:10.1016/0959-437X(95)80055-7. PMID 7549435.
8. Acharya S, et al. (1996). "hMSH2 forms specific mispair-binding complexes with hMSH3 and hMSH6". PNAS. 93 (24): 13629–34. Bibcode:1996PNAS...9313629A. doi:10.1073/pnas.93.24.13629. PMC 19374. PMID 8942985.
9. Friedberg EC, Walker GC, Siede W. (1995). DNA repair and mutagenesis. American Society for Microbiology, Washington DC.
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11. Gradia S, Acharya S, Fishel R (1997). "The human mismatch recognition complex hMSH2-hMSH6 functions as a novel molecular switch". Cell. 91 (7): 995–1005. doi:10.1016/S0092-8674(00)80490-0. PMID 9428522. S2CID 3551402.
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18. Wang Y, Qin J (Dec 2003). "MSH2 and ATR form a signaling module and regulate two branches of the damage response to DNA methylation". Proceedings of the National Academy of Sciences of the United States of America. 100 (26): 15387–92. Bibcode:2003PNAS..10015387W. doi:10.1073/pnas.2536810100. PMC 307577. PMID 14657349.
19. Guerrette S, Wilson T, Gradia S, Fishel R (Nov 1998). "Interactions of human hMSH2 with hMSH3 and hMSH2 with hMSH6: examination of mutations found in hereditary nonpolyposis colorectal cancer". Molecular and Cellular Biology. 18 (11): 6616–23. doi:10.1128/mcb.18.11.6616. PMC 109246. PMID 9774676.
20. Bocker T, Barusevicius A, Snowden T, Rasio D, Guerrette S, Robbins D, Schmidt C, Burczak J, Croce CM, Copeland T, Kovatich AJ, Fishel R (Feb 1999). "hMSH5: a human MutS homologue that forms a novel heterodimer with hMSH4 and is expressed during spermatogenesis". Cancer Research. 59 (4): 816–22. PMID 10029069.
21. Acharya S, Wilson T, Gradia S, Kane MF, Guerrette S, Marsischky GT, Kolodner R, Fishel R (Nov 1996). "hMSH2 forms specific mispair-binding complexes with hMSH3 and hMSH6". Proceedings of the National Academy of Sciences of the United States of America. 93 (24): 13629–34. Bibcode:1996PNAS...9313629A. doi:10.1073/pnas.93.24.13629. PMC 19374. PMID 8942985.
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Dopunska literatura

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Vanjski linkovi

• FAQs on HNPCC Arhivirano 15. 8. 2007. na Wayback Machine from the National Institute of Health
• GeneReviews/NCBI/NIH/UW entry on Lynch syndrome
• MSH6 protein, human na US National Library of Medicine Medical Subject Headings (MeSH)