Characterization and analysis of posttranslational modifications of the human large cytoplasmic ribosomal subunit proteins by mass spectrometry and Edman sequencing.
The 60S ribosomal proteins were isolated from ribosomes of human placenta and separated by reversed phase HPLC. The fractions obtained were subjected to trypsin and Glu-C digestion and analyzed by mass fingerprinting (MALDI-TOF), MS/MS (ESI), and Edman sequencing. Forty-six large subunit proteins were found, 22 of which showed masses in accordance with the SwissProt database (June 2002) masses (proteins L6, L7, L9, L13, L15, L17, L18, L21, L22, L24, L26, L27, L30, L32, L34, L35, L36, L37, L37A, L38, L39, L41). Eleven (proteins L7, L10A, L11, L12, L13A, L23, L23A, L27A, L28, L29, and P0) resulted in mass changes that are consistent with N-terminal loss of methionine, acetylation, internal methylation, or hydroxylation. A loss of methionine without acetylation was found for protein L8 and L17. For nine proteins (L3, L4, L5, L7A, L10, L14, L19, L31, and L40), the molecular masses could not be determined. Proteins P1 and protein L3-like were not identified by the methods applied.
Odintsova
Tatyana I
TI
Vavilov Institute of General Genetics, Russian Academy of Sciences, Moscow, Russian Federation.
Müller
Eva-Christina
EC
Ivanov
Anton V
AV
Egorov
Tsezi A
TA
Bienert
Ralf
R
Vladimirov
Serguei N
SN
Kostka
Susanne
S
Otto
Albrecht
A
Wittmann-Liebold
Brigitte
B
Karpova
Galina G
GG
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D006801:Humans; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011499:Protein Processing, Post-Translational; D012269:Ribosomal Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D020539:Sequence Analysis, Protein
D012269:Ribosomal Proteins