Translational polymorphism as a potential source of plant proteins variety in Arabidopsis thaliana

被引:17
作者
Kochetov, AV
Sarai, A
机构
[1] Russian Acad Sci, Inst Cytol & Genet, Novosibirsk 630090, Russia
[2] Inst Phys & Chem Res, Tsukuba Inst, Tsukuba, Ibaraki 305, Japan
基金
俄罗斯基础研究基金会;
关键词
D O I
10.1093/bioinformatics/btg443
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Motivation: According to scanning model, 40S ribosomal subunits can either initiate translation at start AUG codon in suboptimal context or miss it and initiate translation at downstream AUG(s), thereby producing several proteins. Functional significance of such a protein translational polymorphism is still unknown. Results: We compared predicted subcellular localizations of annotated Arabidopsis thaliana proteins and their potential N-terminally truncated forms started from the nearest downstream in-frame AUG codons. It was found that localizations of full and N-truncated proteins differ in many cases: 12.2% of N-truncated proteins acquired sorting signals de novo and 5.7% changed their predicted subcellular locations (mitochodria, chloroplast or secretory pathway). It is likely that the in-frame downstream AUGs may be frequently utilized to synthesize proteins possessing new functional properties and such a translational polymorphism may serve as an important source of cellular and organelle proteomes.
引用
收藏
页码:445 / 447
页数:3
相关论文
共 17 条
[1]   Biosynthesis of osteogenic growth peptide via alternative translational initiation at AUG85 of histone H4 mRNA [J].
Bab, I ;
Smith, E ;
Gavish, H ;
Attar-Namdar, M ;
Chorev, M ;
Chen, YC ;
Muhlrad, A ;
Birnbaum, MJ ;
Stein, G ;
Frenkel, B .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (20) :14474-14481
[2]   Predicting subcellular localization of proteins based on their N-terminal amino acid sequence [J].
Emanuelsson, O ;
Nielsen, H ;
Brunak, S ;
von Heijne, G .
JOURNAL OF MOLECULAR BIOLOGY, 2000, 300 (04) :1005-1016
[3]   Analysis of the genome sequence of the flowering plant Arabidopsis thaliana [J].
Kaul, S ;
Koo, HL ;
Jenkins, J ;
Rizzo, M ;
Rooney, T ;
Tallon, LJ ;
Feldblyum, T ;
Nierman, W ;
Benito, MI ;
Lin, XY ;
Town, CD ;
Venter, JC ;
Fraser, CM ;
Tabata, S ;
Nakamura, Y ;
Kaneko, T ;
Sato, S ;
Asamizu, E ;
Kato, T ;
Kotani, H ;
Sasamoto, S ;
Ecker, JR ;
Theologis, A ;
Federspiel, NA ;
Palm, CJ ;
Osborne, BI ;
Shinn, P ;
Conway, AB ;
Vysotskaia, VS ;
Dewar, K ;
Conn, L ;
Lenz, CA ;
Kim, CJ ;
Hansen, NF ;
Liu, SX ;
Buehler, E ;
Altafi, H ;
Sakano, H ;
Dunn, P ;
Lam, B ;
Pham, PK ;
Chao, Q ;
Nguyen, M ;
Yu, GX ;
Chen, HM ;
Southwick, A ;
Lee, JM ;
Miranda, M ;
Toriumi, MJ ;
Davis, RW .
NATURE, 2000, 408 (6814) :796-815
[4]  
Kettman JR, 2002, PROTEOMICS, V2, P624, DOI 10.1002/1615-9861(200206)2:6<624::AID-PROT624>3.0.CO
[5]  
2-I
[6]  
Kochetov A. V., 2002, Molekulyarnaya Biologiya (Moscow), V36, P649
[7]   The predicted candidates of arabidopsis plastid inner envelope membrane proteins and their expression profiles [J].
Koo, AJK ;
Ohlrogge, JB .
PLANT PHYSIOLOGY, 2002, 130 (02) :823-836
[8]   Pushing the limits of the scanning mechanism for initiation of translation [J].
Kozak, M .
GENE, 2002, 299 (1-2) :1-34
[9]  
Kruft V, 2001, PLANT PHYSIOL, V127, P1694, DOI 10.1104/pp.010474
[10]   Subcellular localization of the yeast proteome [J].
Kumar, A ;
Agarwal, S ;
Heyman, JA ;
Matson, S ;
Heidtman, M ;
Piccirillo, S ;
Umansky, L ;
Drawid, A ;
Jansen, R ;
Liu, Y ;
Cheung, KH ;
Miller, P ;
Gerstein, M ;
Roeder, GS ;
Snyder, M .
GENES & DEVELOPMENT, 2002, 16 (06) :707-719