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. 2011 May 24;10(9):M110.004739. doi: 10.1074/mcp.M110.004739

Table I. List of the 244 proteins found among the 1116 quantified to significantly change during heat stress. Protein IDs are derived from gene models from version 3.1 of the Chlamydomonas genome sequence (16).

Bin Functional group No of proteins in bin Enrichment (p value)a Ups (Cluster; maximum fold increase)b Downs (Cluster; maximum percent decrease)c
1 Flagellar and basal body proteins 38 1,0E+00 - FAP24(C;40.1), FAP103(D;11.3), FAP278(E;21.5), PF9(-;66.4)
2.0 Other proteins associated with light reactions 19 6,1E-01 LHCSR3(A;1.2), ULP1(B;2.7) FNR1(E;9.4), TEF8(C;45.0)
2.1 Proteins associated with PS I 11 4,0E-01 PSAN(B;2.1), LHCA3(B;1.2) LHCA5(E;16.9)
2.2 Proteins associated with PS II 10 1,3E-01 - PSBO(D;19.1), PSBP1(C;30.7), LHCBM1(C;45.6), LHCBM3(C;35.5)
3 Proteins of photosynthetic and photorespiratory carbon metabolism 30 2,2E-7 - SHMT1(D;25.9), SHMT2(C;13.8), SHMT3(E;9.8), GCST(C;7.1), GCSP(E;11.3), rbcL(D;11.4), RCA1(C;29.6), CP12(D;22.2), FBA3(E;8.1), TRK1(E;9.7), FBP1(E;10.9), SBP1(E;8.7), RPE1(C;26.5), TPIC(E;14.8), PRK1(E;5.9), LCIB(D;8.2), LCIC(D;10.3), LCI23(-;87.2), CAH4(D;12.9), PPD2(C;31.9)
4 Starch synthesis & degradation 8 4,4E-01 - PHOA(D;17.5), PHOB(D;14.6)
5 Porphyrin biogenesis 14 1,7E-01 - GSA(D;17.8), ALAD(D;12.7), UROD1(E;30.9), UROD2(-;82.0), CHLI1(C;18.8)
6 Carotenogenic enzymes 5 - -
7 Glycolysis and gluconeogenesis 13 7,9E-01 - PGH1(D;10.0), PYK1(E;27.0)
8 TCA 14 3,7E-01 - PDC1(D;19.1), IDH3(E;7.2), OGD1(D;19.7), OGD2(D;32.1)
9 Oxidative pentose phosphate pathway 6 6,0E-01 - 101528(E;19.8)
10 Acetate metabolism/glyoxylate cycle 10 6,4E-03 - ACS1(D;15.1), ACS3(D;10.4), ACH1(D;9.2), ICL1(D;21.0), MAS1(D;11.4), MDH1(D;10.8)
11 Fermentation 6 2,8E-01 - PDC3(C;59.1), PFL1(C;67.2)
12 Glycerolipid metabolism 22 5,8E-01 - BCR1(C;20.2), KAR1(E;18.2), ENR1(C;26.1), 190684(C;60.3), ATO1(D;29.7)
13 Mitochondrial electron transport chain and ATP synthase 12 9,6E-01 - CYC(D;36.6)
14 N-metabolism 7 3,3E-03 - GSF1(D;14.2), GSN1(C;32.8), GLN1(E;25.5), 194028(C;22.0), MDH5(E;20.4)
15 Amino acid metabolism 47 1,8E-01 - 136279(E;42.5), 162449(D;21.3), 126232(E;29.0), HIS1(D;43.1), 140252(E;14.0), ASSD1(C;24.2), METE(C;58.6), THS1(D;19.8), AAD1(D;16.1), AAI1(C;22.5), ALSS1(C;17.6), LEU2(E;25.4), AGS1(D;12.3), CMPL1(D;16.7)
16 S-assimilation 5 5,2E-01 - ATS1(C;60.5)
17 Metal handling 3 2,8E-01 - SBD1(E;16.9)
18 C1 metabolism 6 8,7E-03 - FDH1(D;80.2), 111330(C;15.0), METM(C;12.3), SAH1(D;21.6)
19 Vitamin biosynthesis 7 3,7E-01 THI4a(A;1.5) PDX1(C;41.5)
20.0 Protein folding and abiotic stress 8 7,9E-01 154979(A;2.5) -
20.1 Small heat shock proteins 3 0,0E+00 HSP22A(B;21.4), HSP22C(B;26.0), HSP22E(B;13.2) -
20.2 HSP60s 15 6,4E-03 CPN60A(B;4.1), CPN60B1(B;2.1), CPN60B2(B;4.0), CPN60C(A;1.3), CPN23(B;2.5), CPN20(B;2.5), CPN10(B;3.0), CPN11(B;2.5) -
20.3 HSP70 and co-chaperones 11 3,3E-04 HSP70A(B;2.9), HSP70B(B;2.4), HSP70C(B;1.3), HSP70E(B;2.0), 150437(A;6.4), MOT53(-;3.2), DNJ1(A;2.3) HSP70G(E;56.9)
20.4 HSP90 and co-chaperones 5 3,0E-03 HSP90A(B;5.2), HSP90B(B;1.4), HSP90C(B;3.4), HOP1(A;2.6) -
20.5 HSP100 4 8,7E-03 CLPB1(A;22.1), CLPB3(A;5.7), CLPB4(A;6.2) -
20.6 FKBPs/Cyclophilins 10 1,1E-03 FKB62(B;11.5) FKB12(D;17.7), FKB53(E;10.7), CYN19–2(C;43.4), CYN20–1(E;9.0), CYN20–3(C;46.7), CYN38(D;29.3)
21 Proteases/Peptidases 53 1,0E+00 - 82208(E;7.5), 139416(D;18.0), UBC2(D;23.1), CDC48(D;16.8)
22 Redox regulation/oxidative stress response 35 4,1E-01 - TRXH(C;15.4), CITRX(E;8.4), RB60(D;15.3), CCPR1(C;53.4), 165193(E;9.4), APX1(C;36.5), GPX5(E;16.8), FSD1(E;4.9), MSRA4(-;39.2)
23 Nucleotide metabolism 26 1,0E+00 - 175039(D;28.7)
24 Sugar nucleotide metabolism 10 1,3E-01 - 158152(C;23.6), SNE1(E;15.4), SNE6(C;10.8), UPTG1(D;17.6)
25 RNA processing/binding 43 1,0E+00 - RSZ22(C;46.1), UAP56(E;6.0), NOP1(D;43.6), 184151(D;15.9), RB47(D;13.0), RB38(D;16.9)
26 DNA binding/transcription/chromatin remodeling 65 1,0E+00 153995(-;3.3), 24073(B;1.5) GBP1(E;27.1), 186410(C;33.5), 154370(E;16.5)
27.1 Protein biosynthesis (not ribosome) 50 6,0E-01 - 186253(E;23.6), 82920(D;32.6), 38643(E;19.9), 145770(D;14.0), EFG2(D;13.6), EFT1a(C;64.4), tufA(D;13.2), EIF3K(D;19.7), 188942(C;13.9), EIF4E(C;17.1), EIF6A(D;23.4)
27.2.0 Protein biosynthesis 4 - -
27.2.1 Protein biosynthesis (LSU plastid) 21 9,4E-01 - PRPL1(D;37.0), rpl2(E;10.7), PRPL9(E;10.2)
27.2.2 Protein biosynthesis (SSU plastid) 15 - -
27.2.3 Protein biosynthesis (LSU cytosol) 40 1,4E-06 - RPP0(E;7.3), RPL3(D;21.1), RPL4(D;10.5), RPL5(E;5.9), RPL6(E;14.3), RPL7(D;20.6), RPL9(E;6.3), RPL10(D;16.9), RPL10a(D;11.4), RPL12(C;10.4), RPL13(D;13.3), RPL14(D;12.4), RPL18a(D;11.5), RPL19(E;10.3), RPL21(E;8.3), RPL22(E;11.1), RPL27(D;7.9), RPL28(C;14.9), RPL32(D;28.6), RPL35(D;14.1), RPL35a(D;18.9), RPL36(E;15.5), RPL40(E;31.2)
27.2.4 Protein biosynthesis (SSU cytosol) 31 9,4E-09 - RPS2(D;26.9), RPS3(E;13.8), RPS3a(E;15.0), RPS4(D;31.4), RPS6(D;29.5), RPS7(D;26.2), RPS8(D;17.3), RPS9(E;27.1), RPS10(E;14.2), RPS14(C;17.4), RPS15(D;12.1), RPS15a(C;27.6), RPS16(D;18.8), RPS18(D;10.2), RPS19(E;9.2), RPS20(D;15.0), RPS23(D;35.4), RPS24(E;22.5), RPS25(D;17.0), RPS27-A(D;18.0), RPS28(D;13.3), RPS29(D;27.3)
28 Signal transduction 58 1,0E+00 CRT2(B;1.1), AKC2(-;2.0) 184895(D;6.7), RACK1(E;7.3), PP2A-2r(E;21.5), RABC2(-;25.1), FTT1(D;15.2)
29 Pumps and transporters 16 9,4E-01 - ATPvA1(D;16.2), ATPvB(D;10.4)
30 Vesicle transport 22 9,5E-01 - COPE1(E;30.6), COPG1(C;17.1), VPS35(C;18.3)
31 Cytoskeleton 9 - -
32 Miscellaneous 145 1,0E+00 193531(A;43.8), 148088(B;1.6) SPS1(E;21.1), CPLD48(-;35.9), 190138(C;22.5), 190503(C;23.6), RCD2(C;26.0), 194623(C;20.0), 179100(D;54.5)
33 Proteins without functional annotation 115 1,0E+00 - 144849(C;15.6), 178937(C;97.1), 95661(-;30.0), 192803(D;12.6), 137973(-;44.3), CGL13(-;20.7), 166509(-;33.5)
34 Protein sorting 9 9,4E-02 - TIC40(D;46.6), TIC110(-;19.1), SRP19(C;32.6), IPB2(E;23.7)

a Significant bin enrichment is given at p values below 1,0E-02.

b Cluster A = UP fast; B = UP delayed; C = DOWN fast; D = DOWN delayed; E = DOWN delayed, into steady state. Maximum fold increase was calculated by dividing protein quantification values for all time points with the value of the first available time point and selecting the quotient with the highest value for display.

c Maximum percent decrease was calculated by subtracting the quotients of protein quantification values from all time points and the first available time point from 1 and selecting the difference with the highest value for display.