From: Subject: Research News: Revealing the Secrets of WRN Date: Fri, 28 Apr 2006 09:32:52 +0200 MIME-Version: 1.0 Content-Type: multipart/related; type="text/html"; boundary="----=_NextPart_000_0073_01C66AA6.B8AE3DA0" X-MimeOLE: Produced By Microsoft MimeOLE V6.00.2900.2869 This is a multi-part message in MIME format. ------=_NextPart_000_0073_01C66AA6.B8AE3DA0 Content-Type: text/html; charset="iso-8859-1" Content-Transfer-Encoding: quoted-printable Content-Location: http://www.lbl.gov/Science-Articles/Archive/LSD-WRN-secrets.html Research News: Revealing the Secrets of = WRN
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Revealing the Secrets of WRN

The Unique Protein Responsible for = Werner's Syndrome=20 Aids Research in Cancer and Aging

Contact: Paul Preuss, = (510)=20 486-6249, mailto:paul_preuss@lbl.gov?subject=3DRe:=20 Revealing the Secrets of WRN

BERKELEY, CA =97 A team of scientists from Lawrence Berkeley = National=20 Laboratory and the Scripps Research Institute has determined the = crystal=20 structure and molecular mechanisms of a key part of WRN, a protein = that=20 protects humans from premature aging and cancer.  

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The fold structure of the = WRN=20 exonuclease domain, with alpha helices (blue), beta strands = (green),=20 and loops (brown). The active-site amino-acid residues are = at center=20 (yellow), showing oxygen atoms (red) and two manganese ions=20 (magenta).

When the gene for WRN is defective the result is Werner's = syndrome, a=20 rare inherited disease that shows no symptoms until puberty but = soon=20 causes rapid aging. Beginning in their twenties, victims may = become=20 afflicted with cataracts, hair loss, wrinkled skin, osteoporosis,=20 arteriosclerosis, and type II diabetes; many patients contract = cancer, and=20 most die by the age of 50. Understanding how the WRN protein = normally=20 works to maintain genomic integrity could lead to new forms of = treatment=20 for cancer and age-related pathologies.  

"One reason we are particularly interested in WRN is because = Werner's=20 syndrome is unusual among premature-aging diseases, in that = children are=20 born normal and show no signs of disease until early adulthood," = says=20 Steven Yannone of Berkeley Lab's Life Sciences Division. "This = gives us a=20 better chance of clearly separating defects in development from = aging."=20

"We wanted to study the protein itself because it is unique," = says Jeff=20 Perry of the Scripps Research Institute's Department of Molecular = Biology=20 and Skaggs Institute for Chemical Biology, formerly of Berkeley = Lab, who=20 led the research with Yannone. "WRN belongs to a family of enzymes = called=20 RecQ helicases" =97 of which there are five in the human genome, = performing=20 important functions in DNA replication, recombination, and repair = =97 "but=20 in this family, only WRN has coupled a helicase function and a = nuclease=20 function within the same protein."

Helicases open up the double helix of DNA, while nucleases = degrade one=20 or both of the DNA chains; both operations are critical to = repairing=20 errors and proofreading DNA sequences. One part of WRN is an = exonuclease,=20 which starts working from the end of a DNA strand. Perry and = Yannone and=20 their colleagues determined the structure of the WRN exonuclease = domain=20 (WRN-exo) and showed how the enzyme may function in a series of = specific=20 DNA repair events. Their findings will soon appear in Nature=20 Structural & Molecular Biology and are now available = online.

All the members of the research team were participants in the = SBDR=20 program (Structural Cell Biology of DNA Repair Machines) sponsored = by the=20 National Cancer Institute. John Tainer, a professor at Scripps = Research,=20 member of the Skaggs Institute for Chemical Biology, and a = visiting=20 scientist at Berkeley Lab, is SBDR's principal investigator. = Co-principal=20 investigator is Priscilla Cooper, head of the Department of = Molecular=20 Biology in Berkeley Lab's Life Sciences Division.

Tainer says, "The exonuclease domain of the WRN protein is a = prime=20 example of what we in SBDR call 'master keys,' structures that = open doors=20 to lots of different repair pathways. Among other things, WRN is = involved=20 in repairing double-strand breaks, single-strand breaks, = replication forks=20 and junctions, even DNA-RNA duplexes. How does one protein know = how to=20 interact in so many different processes? If we can understand how = this=20 unique protein works, we'll have a key to how all these pathways = work in=20 human beings."

Cooper says, "Understanding the relationship between the = structure of=20 WRN and how it performs its multiple functions to prevent aging = and cancer=20 is a perfect example of the kind of problem we designed the SBDR = program=20 to solve. With 21 investigators in 15 institutions, SBDR's goal is = to gain=20 fundamental insights into the molecular machines that maintain = genomic=20 integrity, by applying a range of experimental = techniques."  =20

Other members of the SBDR team who researched WRN were Lauren = Holden=20 and Chiharu Hitomi of Scripps Research, Aroumougame Asaithamby and = David=20 Chen of the University of Texas Southwestern Medical Center, and = Seungil=20 Han of Pfizer, Inc. Asaithamby, Han, and Chen are former members = of=20 Berkeley Lab; Chen is a senior member of the SBDR program.

Structure Points to Function

Jeff Perry is a specialist in structural biology, including = x‑ray=20 crystallography, and Steve Yannone specializes in biochemistry; = both kinds=20 of expertise are essential to solving the mysteries of WRN. The=20 researchers began by constructing, from recombinant DNA, the = portion of=20 the protein known to have exonuclease activity.

"First we had to find out where the exonuclease region was = within the=20 protein sequence," Perry says. The next step was to grow crystals = of this=20 exonuclease domain. "Only the last of the 10 crystals we had for = phasing =97=20 a crucial step in determining structure =97 worked, so it was a = bit of a=20 cliff-hanger."

Using x-ray crystallography beamlines 5.0.2 and 8.3.1 at = Berkeley Lab's=20 Advanced Light Source, the researchers determined how WRN-exo was = folded.=20 The fold structure revealed that WRN-exo belongs to a family of = nucleases=20 involved in maintaining genomic integrity, the DnaQ family, which = has a=20 long evolutionary history and is found in archaea, bacteria, and = viruses,=20 as well as higher plants and animals. Indeed, WRN-exo is the first = member=20 of the family whose structure has been determined in humans.

The structure of the larger WRN protein is known to be built = from=20 several individual copies of WRN. To determine how individual = WRN-exo=20 units might work together as a complex, the researchers borrowed a = similarly folded DnaQ protein from a plant, Arabidopsis = thaliana=20 ("Mouse-ear cress"), and used it as a template for the likely = higher-order=20 structure. The result was a ring of six WRN exonuclease domains, = just the=20 right size to slip around a DNA helix, with their binding and = catalysis=20 sites oriented inward toward the encircled DNA.

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In this model, six WRN-exo = subunits=20 form a ring of just the right diameter to surround a strand = of DNA.=20 Active sites of the WRN-exo domains face inward, including = the metal=20 ions indicated by spheres.

This ring structure reminded the researchers of another protein = complex=20 called Ku70/80, which like WRN encircles and binds to the ends of = DNA.=20 Also like WRN, Ku70/80 participates in an important form of DNA = repair=20 called nonhomologous end-joining; indeed, biochemical assays = showed that=20 Ku70/80 greatly stimulates this activity in WRN. Structurally, = moreover,=20 the two rings stack neatly together, suggesting that they have = evolved to=20 work together.

"This is an example of how interesting questions of = biochemistry arise=20 from looking at structures," says Yannone.

A prominent feature of the WRN-exo fold was the position of the = two=20 charged atoms of metal it incorporated. "To compare how different = kinds of=20 metal ions affected the activity of WRN-exo, we did both in vitro = and in=20 vivo assays," Yannone says. "In the test tube, manganese ions = showed=20 higher catalytic activity. But magnesium ions are more common in = cells.=20 One or the other is essential if WRN‑exo is to perform its = basic function=20 of editing DNA."

These and other activity assays provided crucial insights into = the=20 relation of structure and function in WRN. In vivo assays were = performed=20 with cell lines, including Werner's syndrome cells, supplied by = Berkeley=20 Lab's Judith Campisi, a leading researcher in aging. The assays = helped to=20 determine just how the WRN-exo domain does its work within the = cell, and=20 how mutations in WRN may interfere with that work.

Campisi says it's tempting to speculate that differences in the = way=20 people age, and how fast they age, could be partly due to = variations in=20 their WRN proteins. "Should this be the case, knowing the = structure=20 of WRN will be crucial for understanding how slight variations in = the=20 protein might alter its function," she says. "Ultimately, = scientists might=20 be able to use the structural data to design drugs to specifically = optimize WRN function, leading to healthier life spans!"

Leading Questions

"How does WRN do what it does? When and where does WRN go to = work?=20 That's the $10 million question," says Perry, "but we're beginning = to=20 answer it."

Their approach is to determine the structure and chemistry of=20 individual parts of the WRN protein and then piece them back = together.=20 "This will let us clearly visualize just how the nuclease and = helicase=20 functions work together," Perry says, "and how they are integrated = into=20 cellular pathways through their interactions with partner = proteins."=20  

Yannone is particularly intrigued by the hope of understanding = why the=20 symptoms of Werner's syndrome don't show up until early adulthood, = even=20 though WRN is a highly versatile protein that would seem to = function at=20 all stages of development. "I suspect that WRN functions in many = cellular=20 processes but is essential to only some of them =97 these unique = functions=20 being the key to its role in aging."

The structure of WRN exonuclease, itself unique, may be a clue = to its=20 selectivity. WRN nuclease is similar to the proofreading domain of = the=20 DnaQ family of DNA polymerases, but the nature of WRN's = interactions with=20 other key proteins may dictate a more complex, higher-order = editing role=20 in maintaining the human genome.

"The modularity of WRN-exo is one of the things that's exciting = to me,"=20 says SBDR's John Tainer. "There are some 30,000 human genes, but = the=20 connections among them are not like a wiring diagram =97 they're = more like=20 the way an airline connects its routes, with many pathways going = through a=20 few major hubs. WRN is one of those hubs."

Priscilla Cooper says, "SBDR investigators and others have = shown that=20 WRN interacts directly with a number of other proteins that have = been=20 implicated in premature aging disorders, some of which probably = constitute=20 other hubs. Ongoing studies of how these hubs connect should yield = further=20 insights into the molecular bases of cancer predisposition and = premature=20 aging."

Additional information

  • "WRN exonuclease structure and molecular mechanism imply an = editing=20 role in DNA end processing," by J. Jefferson P. Perry, Steven M. = Yannone, Lauren G. Holden, Chiharu Hitomi, Aroumougame = Asaithamby,=20 Seungil Han, Priscilla K. Cooper, David J. Chen, and John A. = Tainer,=20 will appear in a forthcoming issue of Nature Structural = &=20 Molecular Biology and is now available online to = subscribers. Go to=20 http://dx.doi.org/ and enter = DOI number=20 10.1038/Nsmb1088.=20
  • The Scripps Research Institute, headquartered in La Jolla,=20 California, is one of the world's largest independent, nonprofit = biomedical research organizations. Visit their website at http://www.scripps.edu/e_ind= ex.html.=20
  • Berkeley Lab is a U.S. Department of Energy national = laboratory=20 located in Berkeley, California. It conducts unclassified = scientific=20 research and is managed by the University of California. Visit = our=20 website at http://www.lbl.gov/.=20
 
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