“AT-hook”的意思、由来-开放百科全书

The AT-hook is a DNA-binding motif present in many proteins, including the high mobility group (HMG) proteins,^[1] DNA-binding proteins from plants ^[2] and hBRG1 protein, a central ATPase of the human switching/sucrose non-fermenting (SWI/SNF) remodeling complex.^[3]

This motif consists of a conserved, palindromic, core sequence of proline-arginine-glycine-arginine-proline, although some AT-hooks contain only a single proline in the core sequence. AT-hooks also include a variable number of positively charged lysine and arginine residues on either side of the core sequence.^[4] The AT-hook binds to the minor groove of adenine-thymine (AT) rich DNA, hence the AT in the name. The rest of the name derives from a predicted asparagine/aspartate "hook" in the earliest AT-hooks reported in 1990.^[5] In 1997 structural studies using NMR determined that a DNA-bound AT-hook adopted a crescent or hook shape around the minor groove of a target DNA strand (pictured at right).^[6] HMGA proteins contain three AT-hooks, although some proteins contain as many as 30.^[5] The optimal binding sequences for AT-hook proteins are repeats of the form (ATAA)_n or (TATT)_n, although the optimal binding sequences for the core sequence of the AT-hook are AAAT and AATT.^[7]

References

1. ^{{cite journal | vauthors = Reeves R, Beckerbauer L | title = HMGI/Y proteins: flexible regulators of transcription and chromatin structure | journal = Biochim. Biophys. Acta | volume = 1519 | issue = 1–2 | pages = 13–29 |date=May 2001 | pmid = 11406267 | doi = 10.1016/S0167-4781(01)00215-9| url = }}
2. ^{{cite journal | vauthors = Meijer AH, van Dijk EL, Hoge JH | title = Novel members of a family of AT hook-containing DNA-binding proteins from rice are identified through their in vitro interaction with consensus target sites of plant and animal homeodomain proteins | journal = Plant Mol. Biol. | volume = 31 | issue = 3 | pages = 607–18 |date=June 1996 | pmid = 8790293 | doi = 10.1007/BF00042233| url = }}
3. ^{{cite journal | vauthors = Singh M, D'Silva L, Holak TA | title = DNA-binding properties of the recombinant high-mobility-group-like AT-hook-containing region from human BRG1 protein | journal = Biol. Chem. | volume = 387 | issue = 10–11 | pages = 1469–78 | year = 2006 | pmid = 17081121 | doi = 10.1515/BC.2006.184 | url = }}
4. ^{{cite journal |doi=10.1016/S0378-1119(01)00689-8 |author=Reeves R |title=Molecular biology of HMGA proteins: hubs of nuclear function |journal=Gene |volume=277 |issue=1–2 |pages=63–81 |date=October 2001 |pmid=11602345 |url=http://linkinghub.elsevier.com/retrieve/pii/S0378111901006898}}
5. ^¹{{cite journal |vauthors=Reeves R, Nissen MS |title=The A.T-DNA-binding domain of mammalian high mobility group I chromosomal proteins. A novel peptide motif for recognizing DNA structure |journal=J. Biol. Chem. |volume=265 |issue=15 |pages=8573–82 |date=May 1990 |pmid=1692833 |url=http://www.jbc.org/cgi/pmidlookup?view=long&pmid=1692833}}
6. ^{{cite journal |vauthors=Huth JR, Bewley CA, Nissen MS |title=The solution structure of an HMG-I(Y)-DNA complex defines a new architectural minor groove binding motif |journal=Nat. Struct. Biol. |volume=4 |issue=8 |pages=657–65 |date=August 1997 |pmid=9253416 |url=http://www.nature.com/nsmb/journal/v4/n8/abs/nsb0897-657.html |doi=10.1038/nsb0897-657|display-authors=etal}}
7. ^{{cite journal|doi=10.2307/3454310 |author=Reeves R |title=Structure and function of the HMGI(Y) family of architectural transcription factors |journal=Environ. Health Perspect. |volume=108 |issue=Suppl 5 |pages=803–9 |date=October 2000 |pmid=11035986 |url=http://www.ehponline.org/members/2000/suppl-5/803-809reeves/reeves-full.html |jstor=3454310 |deadurl=yes |archiveurl=https://web.archive.org/web/20090109141946/http://www.ehponline.org/members/2000/suppl-5/803-809reeves/reeves-full.html |archivedate=2009-01-09 }}