Renaturation of rabbit liver aminoacyl-tRNA synthetases by 80S ribosomes.

Turkovskaya, H. V.; Belyanskaya, Larisa; Kovalenko, M. I.; El'skaya, A. V.

doi:10.1016/s1357-2725(99)00031-x

Cited by 5 publications

(4 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…There is an increasing body of evidence for special structural organization of the protein synthesis machinery in the higher eukaryotic cells. The existence of multimolecular complexes of ARS [1], initiation factors [2] and eEF1 [3,4], ribosome–ARS interactions [5–7], and the association of translation components with cytoskeletal framework [8] are among the important signs of the protein synthesis compartmentalization. Moreover, detailed fluorescence‐based measurements of translation in living dendrites have visualized the mammalian protein synthesis compartments in situ [9].…”

mentioning

confidence: 99%

Novel complexes of mammalian translation elongation factor eEF1A·GDP with uncharged tRNA and aminoacyl‐tRNA synthetase

Petrushenko

Budkevich

Shalak

et al. 2002

European Journal of Biochemistry

View full text Add to dashboard Cite

Multimolecular complexes involving the eukaryotic elongation factor 1A (eEF1A) have been suggested to play an important role in the channeling (vectorial transfer) of tRNA during protein synthesis [Negrutskii, B.S. & El'skaya, A.V. (1998) Prog. Nucleic Acids Res. Mol. Biol. 60, 47–78]. Recently we have demonstrated that besides performing its canonical function of forming a ternary complex with GTP and aminoacyl‐tRNA, the mammalian eEF1A can produce a noncanonical ternary complex with GDP and uncharged tRNA [Petrushenko, Z.M., Negrutskii, B.S., Ladokhin, A.S., Budkevich, T.V., Shalak, V.F. & El'skaya, A.V. (1997) FEBS Lett. 407, 13–17]. The [eEF1A·GDP·tRNA] complex has been hypothesized to interact with aminoacyl‐tRNA synthetase (ARS) resulting in a quaternary complex where uncharged tRNA is transferred to the enzyme for aminoacylation. Here we present the data on association of the [eEF1A·GDP·tRNA] complex with phenylalanyl‐tRNA synthetase (PheRS), e.g. the formation of the above quaternary complex detected by the gel‐retardation and surface plasmon resonance techniques. To estimate the stability of the novel ternary and quaternary complexes of eEF1A the fluorescence method and BIAcore analysis were used. The dissociation constants for the [eEF1A·GDP·tRNA] and [eEF1A·GDP·tRNAPhe·PheRS] complexes were found to be 20 nm and 9 nm, respectively. We also revealed a direct interaction of PheRS with eEF1A in the absence of tRNAPhe (Kd = 21 nm). However, the addition of tRNAPhe accelerated eEF1A·GDP binding to the enzyme. A possible role of these stable novel ternary and quaternary complexes of eEF1A·GDP with tRNA and ARS in the channeled elongation cycle is discussed.

show abstract

mentioning

confidence: 99%

Novel complexes of mammalian translation elongation factor eEF1A·GDP with uncharged tRNA and aminoacyl‐tRNA synthetase

Petrushenko

Budkevich

Shalak

et al. 2002

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

“…Alternatively, issues of co-regulation and availability of sufficient scaffolding might not permit the assembly of such a large complex. Early studies suggested the presence of a complex containing all twenty ARSs; however, the evidence, based exclusively on size fractionation, was also consistent with transient and indirect interactions of all ARSs via translating ribosomes, rather than in a single pansynthetase complex [46-50]. Even if such a large, loosely assembled complex of all 20 ARSs does exist, the nine MARS synthetases might serve as the stable core complex, and the same evolutionary pressures described here would be responsible for selection of synthetases for the core complex.…”

Section: Discussionmentioning

confidence: 99%

Citric acid cycle and the origin of MARS

Eswarappa

Fox

2013

Trends in Biochemical Sciences

View full text Add to dashboard Cite

The vertebrate multi-aminoacyl tRNA synthetase complex (MARS) is an assemblage of nine aminoacyl tRNA synthetases (ARSs) and three non-synthetase scaffold proteins, AIMP1 (aminoacyl tRNA synthetase complex-interacting multifunctional protein-1), AIMP2, and AIMP3. The evolutionary origin of the MARS is unclear, as is the significance of the inclusion of only nine of twenty tRNA synthetases. Eight of the nine amino acids corresponding to ARSs of the MARS are derived from two citric acid cycle intermediates, α-ketoglutatrate and oxaloacetate. We propose that the metabolic link with the citric acid cycle, the appearance of scaffolding proteins AIMP2 and AIMP3, and the subsequent disappearance of the glyoxylate cycle, together facilitated the origin of the MARS in a common ancestor of metazoans and choanoflagellates.

show abstract

“…Ніякого впливу цих молекул на активність АРСаз за даних умов не виявлено. Проаналізовано всі можливі механізми стимулювального впливу рибосом [20,21 ]. Зроблено висновок, що зростання активності частково денатурованого ферменту в присутності рибосом може бути результатом відновлення його активної конформації і, отже, рибосоми виконують функцію, подібну до молекулярних шаперонів.…”

unclassified

Chaperone-like properties of the protein synthesis components

Lukash

Turkivska

2005

Biopolym. Cell

View full text Add to dashboard Cite

Розглянуто і проаналізовано роботи, присвячені дослідженню ишпероноподібних властивостей рибосом та окремих білкових факторів трансляції. Крім участі у біосинтезі білка, про-і еукаріотні рибосоми, фактори елонгації ЕР1А, Ер2, еЕРІА та фактор ініціації ІР2 здатні відновлювати активність частково денатурованих ферментів та захищати їх від денатурації. Передбачається, що завдяки шапероноподібним властивостям перелічені компоненти білок синтезувальної системи можуть брати участь у фолдингу чи ренатурації білків та підтримувати їхню продуктивну конформацію у цитоплазмі клітин Ключові слова: молекулярні шаперони, фолдинг, білоксинтезувальна система, рибосоми, білкові фактори трансляції.

show abstract

Renaturation of rabbit liver aminoacyl-tRNA synthetases by 80S ribosomes.

Cited by 5 publications

References 24 publications

Novel complexes of mammalian translation elongation factor eEF1A·GDP with uncharged tRNA and aminoacyl‐tRNA synthetase

Novel complexes of mammalian translation elongation factor eEF1A·GDP with uncharged tRNA and aminoacyl‐tRNA synthetase

Citric acid cycle and the origin of MARS

Chaperone-like properties of the protein synthesis components

Contact Info

Product

Resources

About