Kristensen P, Lund A, Clark B F, Cavallius J, Merrick W C
Department of Chemistry, University of Aarhus, Denmark.
Biochem Biophys Res Commun. 1998 Apr 28;245(3):810-4. doi: 10.1006/bbrc.1998.8510.
The peptide elongation factor 1 alpha (EF-1 alpha) has been isolated and characterised from a number of species. Recently we and others have reported the existence of an isoform of the ubiquitously expressed EF-1 alpha mRNA in higher eukaryotes, including human cells. This isoform has a tissue specific expression pattern, confining it primarily to muscle, heart, and brain. In the present study we have purified the isoform of EF-1 alpha from rabbit muscle. Using partial amino acid analysis, we can conclude that in rabbit muscle essentially only the isoform of elongation factor 1 alpha, designated EF-1 alpha 2, is translated. Preliminary activity assays show that the isoform has the same functional activities as the normal EF-1 alpha, designated EF-1 alpha 1, in relation to protein synthesis, but may behave differently in the ability to bind nucleotides. Based on the availability of the isoforms of EF-1 alpha purified from a mammalian species, it will be possible to conduct further comparative studies in order to elucidate the different functions of EF-1 alpha 1 and EF-1 alpha 2 proteins.
肽链延长因子1α(EF-1α)已从多个物种中分离并鉴定出来。最近,我们和其他人报道了在包括人类细胞在内的高等真核生物中普遍存在的EF-1α mRNA的一种同工型。这种同工型具有组织特异性表达模式,主要局限于肌肉、心脏和大脑。在本研究中,我们从兔肌肉中纯化了EF-1α的同工型。通过部分氨基酸分析,我们可以得出结论,在兔肌肉中基本上只翻译了延长因子1α的同工型,即EF-1α 2。初步活性测定表明,该同工型在蛋白质合成方面与正常的EF-1α(即EF-1α 1)具有相同的功能活性,但在结合核苷酸的能力方面可能表现不同。基于从哺乳动物物种中纯化得到的EF-1α同工型,有可能进行进一步的比较研究,以阐明EF-1α 1和EF-1α 2蛋白的不同功能。