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Originally=20 published in Science Express as 10.1126/science.1091403 on = January=20 2, 2004
Science, Vol. = 303, Issue=20 5657, 540-543, January 23, 2004
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A Map of the Interactome Network of the Metazoan C.=20 elegans

Siming = Li,1*=20 Christopher M. Armstrong,1*=20 Nicolas Bertin,1*=20 Hui Ge,1*=20 Stuart Milstein,1*=20 Mike Boxem,1*=20 Pierre-Olivier Vidalain,1*=20 Jing-Dong J. Han,1*=20 Alban Chesneau,1,2*=20 Tong Hao,1 Debra S.=20 Goldberg,3 Ning = Li,1=20 Monica Martinez,1 = Jean-Fran=E7ois=20 Rual,1,4 Philippe=20 Lamesch,1,4 Lai = Xu,5 Muneesh = Tewari,1=20 Sharyl L. Wong,3 Lan V.=20 Zhang,3 Gabriel F.=20 Berriz,3 Laurent = Jacotot,1 Philippe = Vaglio,1 J=E9r=F4me = Reboul,1 Tomoko=20 Hirozane-Kishikawa,1 Qianru=20 Li,1 Harrison W. = Gabel,1=20 Ahmed Elewa,1||=20 Bridget Baumgartner,5 Debra J. = Rose,6 Haiyuan = Yu,7=20 Stephanie Bosak,8 Reynaldo=20 Sequerra,8 Andrew = Fraser,9=20 Susan E. Mango,10 William M.=20 Saxton,6 Susan = Strome,6=20 Sander van den Heuvel,11 Fabio = Piano,12 Jean=20 Vandenhaute,4 Claude=20 Sardet,2 Mark = Gerstein,7=20 Lynn Doucette-Stamm,8 Kristin = C.=20 Gunsalus,12 J. Wade = Harper,5 Michael E.=20 Cusick,1 Frederick P.=20 Roth,3 David E. Hill,1=B6<= /A>=20 Marc Vidal1=B6<= /A>#=20

To initiate studies on how protein-protein interaction = (or=20 "interactome") networks relate to multicellular=20 functions, we have mapped a large fraction of the = Caenorhabditis elegans interactome network.=20 Starting with a subset of metazoan-specific proteins, = more=20 than 4000 interactions were identified from=20 high-throughput, yeast two-hybrid (HT=3DY2H) = screens.=20 Independent coaffinity purification assays = experimentally=20 validated the overall quality of this Y2H data = set.=20 Together with already described Y2H interactions = and=20 interologs predicted in silico, the current version = of=20 the Worm Interactome (WI5) map contains 3D~=205500=20 interactions. Topological and biological features = of this=20 interactome network, as well as its integration = with=20 phenome and transcriptome data sets, lead to = numerous=20 biological hypotheses.

1 Dana-Farber Cancer Institute and Department = of=20 Genetics, Harvard Medical School, 44 Binney Street, Boston, = MA=20 02115, USA.
2 Institut de G=E9n=E9tique = Mol=E9culaire,=20 Centre National de la Recherche Scientifique UMR 5535, 1919 = Route de=20 Mende, 34293 Montpellier Cedex 5, France.
3 = Department=20 of Biological Chemistry and Molecular Pharmacology, Harvard = Medical=20 School, 250 Longwood Avenue, Boston, MA 02115, = USA.
4=20 Unit=E9 de Recherche en Biologie Mol=E9culaire, Facult=E9s = Notre-Dame de=20 la Paix, 61 Rue de Bruxelles, 5000 Namur, = Belgium.
5=20 Verna and Marrs Department of Biochemistry and Molecular = Biology,=20 Program in Cell and Molecular Biology, Biophysics, and = Biology,=20 Baylor College of Medicine, One Baylor Plaza, Houston, TX = 77030,=20 USA.
6 Department of Biology, Indiana = University,=20 Jordan Hall 142, 1001 East Third Street, Bloomington, IN = 47405,=20 USA.
7 Department of Molecular Biophysics and=20 Biochemistry and Department of Computer Science, Yale = University,=20 266 Whitney Avenue, New Haven, CT 06520, = USA.
8=20 Agencourt Bioscience Corporation, 100 Cummings Center, Suite = 107G,=20 Beverly, MA 01915, USA.
9 The Wellcome Trust = Sanger=20 Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge, = CB10=20 1SA, UK.
10 Huntsman Cancer Institute, = University of=20 Utah, 2000 Circle of Hope, Salt Lake City, UT 84112,=20 USA.
11 Massachusetts General Hospital Cancer = Center,=20 Building 149, 13th Street, Charlestown, MA 02129,=20 USA.
12 Department of Biology, New York = University,=20 1009 Silver Building, 100 Washington Square East, New York, = NY=20 10003, USA.=20


* These authors = contributed equally to this work.

3D{dagger}=20=20 Present address: Department of Pathology, Harvard Medical=20 School, 200 Longwood Avenue, Boston, MA 02115, = USA.=20

3D{ddagger}=20=20 Present address: Modul-Bio, 232 Boulevard = Sainte-Marguerite,=20 13009 Marseille, France.

3D=A7=20=20 Present address: INSERM, Unit=E9 119, Institut Paoli = Calmettes,=20 13009 Marseille, France.

|| Present = address:=20 Program in Gene Function and Expression, University = of=20 Massachusetts, 55 Lake Avenue, North Worcester, MA = 01605,=20 USA.

=B6 Present = address: Center=20 for Cancer Systems Biology and Department of = Cancer=20 Biology, Dana-Farber Cancer Institute and Department = of=20 Genetics, Harvard Medical School, 44 Binney Street, = Boston,=20 MA 02115, USA.

# To whom = correspondence=20 should be addressed. E-mail: marc_vidal@dfci.harvard.edu.=20

To further understand biological processes, it is = important=20 to consider protein functions in the context of = complex=20 molecular networks. The study of such networks = requires=20 the availability of proteome-wide protein-protein = interaction, or "interactome," maps. The yeast=20 Saccharomyces cerevisiae has been used to = develop=20 a eukaryotic unicellular interactome map (= 1=96= 6).=20 Caenorhabditis elegans is an ideal model = for=20 studying how protein networks relate to = multicellularity.=20 Here we investigate its interactome network with=20 HT-Y2H.

As Y2H baits, we selected a set of 3024 worm predicted=20 proteins that relate directly or indirectly to=20 multicellular functions (= 7).=20 Gateway-cloned open reading frames (ORFs) were = available=20 in the C. elegans ORFeome 1.1 (= 8)=20 for 1978 of these selected proteins. Of these, 81 = autoactivated the Y2H GAL1::HIS3 reporter = gene as=20 Gal4 DNA binding domain fusions (DB-X), and 24 others=20 conferred toxicity to yeast cells. The remaining 1873=20 baits were screened against two different Gal4 = activation=20 domain libraries (AD-wrmcDNA and AD-ORFeome1.0), = each=20 with distinct, yet complementary, advantages (= 7).=20

We maximized the specificity of the Y2H system by = applying=20 stringent experimental and bioinformatics = criteria (fig.=20 S1). To eliminate interactions that originated = from=20 nonspecific promoter activation, we only = considered=20 DB-X=96AD-Y pairs if they activated at least two = out of=20 three different Gal4-responsive promoters. = Positives were=20 subsequently retested in fresh yeast cells, and = their=20 AD-Y identities were determined with interaction = sequence=20 tags (ISTs) obtained by sequencing the corresponding=20 polymerase chain reaction (PCR) products (= 9).=20 The AD-Y reading frame was verified for each IST = to avoid=20 the recovery of out-of-frame peptides. In total, = 16,000=20 ISTs were obtained.

Having applied those criteria, we subdivided the=20 interactions into three confidence classes (fig. = S1):=20 those that were found at least three times = independently=20 and for which the AD-Y junction is in frame = ("Core-1,"=20 858 interactions); those in frame found fewer = than three=20 times and that passed the retest ("Core-2," 1299=20 interactions); and all other Y2H interactions found in=20 our screens ("Non-Core," 1892 interactions). The Core = data=20 set (Core-1 and Core-2) contains 2157 = high-confidence=20 interactions between 502 DB-X baits and 1039 AD-Y = preys.=20 After collapsing 22 interactions that occur in = both=20 DB-X=96AD-Y and DB-Y=96AD-X configurations, a = total of 2135=20 unique interactions are obtained (table S1). The = Non-Core=20 data set contains 1892 interactions between 531 = DB-X=20 baits and 1395 AD-Y preys. Altogether, Core and = Non-Core=20 constitute the "First-Pass" data set, with a total = of=20 4027 distinct interactions. Out of 2783 and 1505 = interactions=20 found with AD-wrmcDNA and AD-ORFeome1.0, respectively, = 239=20 interactions were identified with both = libraries.=20

To estimate the coverage of the HT-Y2H data sets, we=20 manually searched the baits screened here for = known=20 interactors in WormPD (10).=20 This search gave rise to 108 interactions, referred to = as=20 the "literature" data set (table S1). The Core and = Non-Core=20 data sets recapitulated eight and two interactions in = this=20 benchmark data set, respectively. Thus, our = overall rate=20 of coverage for the First-Pass data set is 3D~=2010% [(8 +=20 2)/108)].

To evaluate the accuracy of the HT-Y2H data sets, we=20 reasoned that interactions detected in two = different=20 binding assays are unlikely to be experimental=20 false-positives. A representative sample of Y2H=20 interaction pairs from each of these three subsets = (33=20 for Core-1, 62 for Core-2, and 48 for Non-Core) was = randomly=20 selected, and tested in a coaffinity purification = (co-AP)=20 glutathione S-transferase (GST) pull-down = assay=20 (Fig= .=20 1). Bait and prey ORFs were transiently = transfected=20 into 293T cells as GST-bait and Myc-prey fusions, = respectively. For potential interaction pairs = where both=20 proteins were expressed at detectable levels, the = co-AP=20 success rates were 14 out of 17 (82%) for Core-1, = 17 out=20 of 29 (59%) for Core-2, and 8 out of 23 (35%) for = Non-Core=20 (table S2). These data demonstrate that our three data = sets contain a large proportion of highly = reliable=20 interactions and corroborate their expected = relative=20 qualities.

= Fig. 1.=20 Coaffinity purification assays. Shown are 10 examples = from the=20 Core-1, Core-2, and Non-Core data sets. The top panels = show=20 Myc-tagged prey expression after affinity purification = on=20 glutathione-Sepharose, demonstrating binding to = GST-bait. The=20 middle and bottom panels show expression of Myc-prey = and=20 GST-bait, respectively. The lanes alternate between = extracts=20 expressing GST-bait proteins (+) and GST alone (=96). = ORF pairs=20 are identified in table S1 with the lane number = corresponding=20 to the order in which they appear in the table. = [Vi= ew=20 Larger Version of this Image (60K GIF = file)]=20

In addition to experimental screens, we also performed = in=20 silico searches for potentially conserved=20 interactions, or "interologs," whose orthologous = pairs=20 are known to interact in one or more other = species (= 9,=20 11).=20 Starting from a high-confidence yeast interaction = data=20 set (= 7),=20 reciprocal best-hit BLAST searches = (E-value =20 10=966) were performed against the worm = predicted=20 proteome. In all, 949 potential worm interologs were=20 identified, constituting the interologs data set = (= 7).=20 In addition, the Y2H interactome maps that have = been=20 previously generated for individual biological = processes=20 (including vulval development, protein = degradation, DNA=20 damage response, and germline formation) (= 9,=20 12=9614)=20 were pooled to define the "scaffold" data set. = The=20 HT-Y2H, literature, interologs, and scaffold data sets = were=20 combined into Worm Interactome version 5 (WI5), = containing=20 5534 interactions and connecting 15% of the C. = elegans proteome (table S1). WI5 gives rise = to a=20 giant network component of 2898 nodes connected = by 5460=20 edges (Fig= .=20 2A). Similar to other biological networks (15),=20 the worm interactome network exhibits small-world = and=20 scale-free properties (Fig= .=20 2B) (= 7).=20 This data set also allowed us to analyze whether = or not=20 evolutionary recent proteins tend to = preferentially=20 interact with each other rather than with ancient = proteins. We subdivided the nodes of the network = into=20 three classes: 748 proteins with a clear ortholog in = yeast=20 ("ancient"), 1314 proteins with a clear ortholog in=20 Drosophila, Arabidopsis, or humans but not = in=20 yeast ("multicellular"), and 836 proteins with no = detectable ortholog outside of C. elegans = ("worm")=20 (= 7).=20 These three groups seem to connect equally well = with each=20 other (Fig= .=20 2C), which suggests that new cellular = functions rely=20 on a combination of evolutionarily new and ancient=20 elements, consonant with the classic proposal of = evolution=20 as a tinkerer that modifies and adds to = pre-existing=20 structures to create new ones (16).=20

= Fig. 2.=20 Analysis of the WI5 network. (A) Nodes = (representing=20 proteins) are colored according to their phylogenic = class:=20 ancient (red), multicellular (yellow), and worm = (blue). Edges=20 represent protein-protein interactions. The inset = highlights a=20 small part of the network. (B) The proportion = of=20 proteins, P(k), with different numbers of = interacting=20 partners, k, is shown for C. elegans = proteins=20 used as baits or preys and for S. cerevisiae = proteins.=20 (C) The pie charts show the proportion of = interacting=20 preys found in Y2H screens that fall into each = phylogenic=20 class. Also shown is the distribution of all preys = found and=20 all preys searched in the AD-ORFeome 1.0 library. = (D)=20 Overlap with transcriptome (see text) (18),=20 Pearson correlation coefficients (PCCs) were = calculated and=20 graphed for each pair of proteins in the interaction = data sets=20 and their corresponding randomized data sets. The red = area to=20 the right corresponds to interactions that show a = significant=20 relationship to expression profiling data (P = <=20 0.05). (E) Interactions between proteins in = Topomap=20 mountain 29 (18).=20 The dash-circled proteins belong to the same = paralogous family=20 (sharing more than 80% homology) and are thus = collapsed into=20 one set of interactions. (F) Proportion of = interaction=20 pairs where both genes are embryonic lethal (P = <=20 10=967). [Vi= ew=20 Larger Version of this Image (57K GIF = file)]=20

Previous studies have related interactome data with=20 genome-wide expression (transcriptome) and = phenotypic=20 profiling (phenome) data in S. cerevisiae = (17).=20 To investigate to what extent different = functional=20 genomic assays should correlate in the context of = a=20 multicellular organism, we overlapped WI5 with C.=20 elegans transcriptome and phenome data = sets.=20

Based on a C. elegans transcriptome compendium = data set=20 (18),=20 we calculated Pearson correlation coefficients (PCCs) = for=20 gene pairs involved in Y2H interactions and = compared them=20 with randomized data sets (Fig= .=20 2D). About 150 Core interactions (9.5%) = corresponded=20 to gene pairs with significantly higher PCCs than = expected=20 from random (P < 0.05) (table S3). = Thus, those=20 pairs can be considered "more biologically = likely"=20 because two completely independent approaches = point to a=20 functional relationship between the corresponding = genes.=20 The remaining pairs are labeled "without additional = evidence."=20 Indeed, it is important to note that lack of = coexpression=20 does not suggest that the corresponding = interactions are=20 irrelevant. Indeed, 75% of literature pairs, = defined as=20 biologically relevant, do not correlate with=20 transcriptome data (Fig= .=20 2D).

We also systematically examined Y2H interactions where = both=20 proteins belong to common C. elegans expression = clusters, or "Topomap mountains" (18).=20 As an example, a highly connected subnetwork = derived from=20 mountain 29 (Fig= .=20 2E) contains seven proteins (ABU-1, ABU-8, = ABU-11,=20 PQN-5, PQN-54, PQN-57, and PQN-71) that share = common=20 domains (DUF139 domain and cysteine-rich repeat).=20 Furthermore, these proteins are all expressed in the=20 pharynx (19=9621),=20 which suggests that they may act together in = pharynx=20 function or development.

For relatively small-scale S. cerevisiae and C. = elegans interactome data sets, physical = interactions=20 pointed to genes that share similar phenotypes = when=20 knocked out or knocked down (17).=20 To evaluate this idea for the C. elegans=20 interactome, we assembled a collection of = phenotypic data=20 based on RNA interference (RNAi) knockdown = experiments=20 from WormBase (= 7,=20 22),=20 and we calculated the percentage of protein = interaction=20 pairs that share embryonic lethal phenotypes for = the=20 interaction data sets and their randomized = controls and=20 found a twofold enrichment for the Core and First-Pass=20 data sets (Fig= .=20 2F). Similar correlations were also observed = for the=20 maternal sterile phenotype and four groups of = postembryonic=20 phenotypes (23).=20 Because protein-protein interactions for which = both genes=20 are coexpressed across many conditions and show similar = phenotype(s) when knocked down should be considered=20 particularly likely, the global correlations = described=20 above illustrate how biological hypotheses can be = derived=20 from overlapping interactome, transcriptome, and = phenome=20 data sets (table S3).

In S. cerevisiae, two proteins that have many = interaction=20 partners in common are more likely to be related=20 biologically (24).=20 We examined the C. elegans interactome = network for=20 the presence of highly connected neighborhoods by = determining the mutual clustering coefficient = between=20 proteins in the network (table S4) (24).=20 As an example, we examined the properties of one of = the=20 clusters containing such a high-scoring protein pair:=20 VAB-3/C49A1.4 (Fig= .=20 3). VAB-3 and C49A1.4 have strong similarity to the=20 products of the Drosophila genes = eyeless=20 (ey) and eyes absent (eya),=20 respectively, but not to each other. EY and EYA are=20 components of a conserved network of = transcription=20 factors that regulate eye development (25).=20

= Fig. 3.=20 Graphical representation of a highly interconnected = subnetwork=20 around VAB-3 and C49A 1.4. Biological functional = classes were=20 obtained from WormPD (10).=20 [Vi= ew=20 Larger Version of this Image (65K GIF = file)]=20

VAB-3 and C49A1.4 are part of a highly interconnected=20 subnetwork in WI5 (Fig= .=20 3) with proteins that are known or suspected to = be=20 functionally linked to VAB-3 and C49A1.4, or to their=20 respective orthologs in other organisms. These = include=20 (i) EGL-27, which negatively regulates MAB-5 in=20 hermaphrodites (26)=20 and is linked to MAB-5 through C49A1.4; (ii) = WRT-2, an=20 interactor of C49A1.4 with similarity to=20 Drosophila Hedgehog, which alleviates repression = of eya expression by Cubitus interruptus = (27);=20 and (iii) CEH-33 and CEH-35, two of four members = of the=20 sine oculis homeobox gene family, which is = involved in the same Drosophila regulatory = network=20 of transcription factors as ey and eya (28).=20 Finally, eight proteins in this cluster are = annotated in=20 WormPD as involved in membrane function, which = suggests a=20 functional relationship between the = eyeless=20 transcription network and membrane activity.

Together with interologs and previously described=20 interactions, the Y2H data set provides = functional=20 hypotheses for thousands of uncharacterized = proteins in=20 the C. elegans proteome. Integration with = other=20 functional genomic data indicates that the correlation=20 between transcriptome and interactome data, although=20 significant, is lower than what would be expected = from=20 observations made in yeast (17).=20 This observation applies to both the Y2H data set = described here and well-characterized worm interactions = from the literature-derived data set (Fig= .=20 2D). This may occur because, unlike = unicellular=20 organisms, metazoans are complicated by the fact = that=20 biological processes may occur differently in the = organism, across various organs, tissues, or single = cells.=20

Our current interactome map also illustrates how a human=20 interactome project would benefit from an ORFeome = cloning=20 project using recombinational cloning systems, = such as=20 Gateway (= 8).=20 Indeed, recombinationally cloned ORFs can be = shuffled at=20 will into various expression vectors needed for = different=20 types of protein interaction assays, as = exemplified by=20 our ability to transfer bait- and prey-encoding = ORFs into=20 Myc- and GST-tagged vectors to validate Y2H=20 interactions.


References and=20 Notes

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23. H. Ge, unpublished = observations.
24. D. S. Goldberg, F. P. = Roth, Proc.=20 Natl. Acad. Sci. U.S.A. 100, 4372 = (2003).[Abstract/Free = Full Text]
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29. We thank members of M.V.'s = laboratory for their input and help; C. Boone, G. = Achaz and D.=20 Allinger for discussions; the sequencing staff at = Agencourt=20 Biosciences for technical assistance; the ORFeome = meeting=20 participants for their input; C. McCowan, T. = Clingingsmith,=20 and C. You for administrative assistance; and C. = Fraughton for=20 laboratory support. This work was supported by a grant = from=20 NHGRI and NIGMS awarded to M.V. Other support includes = an NSF=20 award (K.C.G.); NIGMS grants (S.v.d.H., S.E.M., = J.W.H.); a=20 Department of Defense Predoctoral Fellowship (B.B.); = an award=20 from the Ligue Nationale Contre Le Cancer (=E9quipe = labelis=E9e)=20 (C.S., A.C.); an institutional HHMI grant (F.P.R., = G.F.B); and=20 Fellowships from EMBO (P.-O.V.), NSF (D.S.G), Ryan, = Milton=20 (S.L.W.), Fu (L.V.Z.), and Leukemia Research = Foundation=20 (M.E.).

Supporting Online = Material=20

www.scien= cemag.org/cgi/content/full/1091403/DC1=20

Material and Methods

Fig. S1

Table S1 to S5

References

11 September 2003; accepted 1 December=20 2003
10.1126/science.1091403
Include this information = when=20 citing this paper.

A= bstract=20 of this Article
PDF=20 Version of this Article
Supportin= g=20 Online Material
 
Down= load=20 to Citation Manager
Alert me when:
new articles cite this=20 article
 
Search for similar articles in:=20
  Science Online=20
  PubMed
Search Medline for articles by:
Li,=20 S. || Vidal,=20 M.
 
This=20 article appears in the following Subject=20 Collections:
Genetics=20
 
All=20 Versions of this Article:
  303/5657/540 (most = recent)
  1091403v1<= /A>
Volume 303, Number 5657, Issue of = 23 Jan 2004,=20 pp. 540-543.
Copyright =A9 2004 by The American Association for = the=20 Advancement of Science. All rights reserved.=20

3D"Functional 3DGrantsNet=20 =



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