Table I.

Identification of Arabidopsis r-proteins by MS analysis

Arabidopsis r-protein identification follows the universally accepted nomenclature as outlined in Barakat et al. (2001). R-proteins resolved in 2 gel spots are designated (1) and (2). Evolutionarily distinct r-proteins are designated (I) and (II). Gel System abbreviations: 1D, 1D SDS polyacrylamide; B, 2D basic-urea; N, 2D nonequilibrium pH. Protein identification method abbreviations: M, MALDI-TOF MS; QT, oMALDI or electro-spray ionization Q-TOF MS/MS; LC/MS/MS, ribosomal and nonribosomal protein complexes were separated by Suc density centrifugation and polysomal proteins separated by 1D SDS-PAGE were digested with trypsin and analyzed; all r-proteins were identified in the Suc gradient purified polysome fraction by LC/MS/MS except P1, P3, L3, L10a, L27a, L28, L30, L35a, L37, and L38.

Small Subunit ProteinsLarge Subunit Proteins
Ribosomal Protein IDGel SystemID MethodSequence CoverageMolecular MassRibosomal Protein IDGel SystemID MethodSequence CoverageMolecular Mass
CalculatedApparentCalculatedApparent
%kD%kD
Sa1DLC/MS/MS3830.0–32.335.0–45.0aP0 (1)NM1433.7–34.443.0
S2BM2730.1–30.937.0P0 (2)NM2633.7–34.444.0
S3NM3827.3–27.536.0P1NQTc11.0–11.217.5
S3aNM3429.8–29.935.0P2 (I)NM5011.0–11.816.5
S4BM, QT5029.8–30.134.0P2 (II)NM7011.0–11.815.5
S5 (1)NM, QT2222.9–23.026.5P3NM3611.8–11.919.0
S5 (2)NM, QT1522.9–23.024.5L3BM4544.5–44.651.0
S6 (1)bBM, QT4128.1–28.434.5L4BM4444.750.0
S6 (2)bBM, QT4128.1–28.434.0L5 (1)NM3034.2–34.440.5
S7 (1)B, NM3421.9–22.227.0L5 (2)NM2134.2–34.439.5
S7 (2)B, NM2821.9–22.225.5L6 (1)BM3726.0–26.236.0
S8BM4223.8–24.132.5L6 (2)BM2526.0–26.230.0
S9BM3123.0–23.227.0L7BM3528.1–28.532.5
S10B, NM4019.4–19.821.5L7aBM2329.0–29.134.0
S11 (1)BM4717.7–18.021.5L8BM4027.9–28.034.5
S11 (2)BM3317.7–18.019.0L9B, NM3522.025.5
S12NQTc15.3–15.418.5L10BM4524.1–24.930.0
S13BM5716.9–17.020.5L10a (1)BM5224.3–24.534.0
S14BM3516.2–16.319.5L10a (2)BM4324.3–24.531.5
S15BM2916.8–17.122.0L11BM5420.9–21.122.5
S15a (I)BM4514.7–15.316.5L12B, NM, QT3117.8–18.021.5
S15a (II)BM6114.7–15.315.5L13BM4523.5–23.831.5
S16BM5616.619.0L13aBM4323.5–23.623.5
S17BM411615.5L14BM3815.518.0
S18 (1)BM4817.518.5L15BM3224.230.0
S18 (2)BQTc17.515.0L17 (1)BM4619.3–19.924.0
S19 (1)BM5715.7–15.816.5L17 (2)BM4119.3–19.924.0
S19 (2)BM5315.7–15.818.0L18 (1)BM4320.8–20.924.5
S20BM3813.1–13.714.0L18 (2)BM4120.8–20.926.5
S21NQTc9.0–9.114.0L18aBM4821.3–21.425.5
S23BM3615.8–16.219.0L19 (1)BQTc23.3–24.636.0
S24BM3015.418.5L19 (2)BQTc23.3–24.634.0
S25 (1)BM3412.114.5L21BM, QT1518.724.0
S25 (2)BM3612.111.0L22BM5014.0–14.517.5
S26BM4514.6–14.818.5L23BM6314.5–15.017.5
S271DLC/MS/MSc9.50.0–14.0aL23aBM4517.4–17.919.0
S27aBQTc17.7–17.814.5L24BM3618.4–18.619.5
S28BM377.3–7.410.5L26 (1)BM6416.8–16.922.0
L26 (2)BM5316.8–16.919.0
L27BM2815.5–15.618.5
L27aBM5616.3–16.519.5
L28BM5415.918.5
L30BM5212.3–12.416.0
L31 (1)BM, QT2113.7–13.820.0
L31 (2)BM1913.7–13.820.0
L32BM3214.5–15.519.5
L34NM3613.6–13.720.0–25.0a
L35BM4314.2–14.318.5
L35aBM2512.8–12.915.5
L36NM3912.2–12.714.0–20.0a
L37BM4410.6–10.812.5
L37a1DLC/MS/MS10.0–10.40.0–14.0a
L38BM608.111.5
L401DLC/MS/MS14.70.0–14.0a
  • a Proteins identified from the 1D gel were from gel slices that had a range in apparent molecular mass.

  • b Multiple isoforms of S6 were detected in both the rapid mobility group and the slow mobility group.

  • c Identification from sequencing one or more peptide.