Mamit-tRNA, a database of mammalian mitochondrial tRNA primary and secondary structures
نویسندگان
چکیده
منابع مشابه
Aminoacyl-tRNA synthetases database
Aminoacyl-tRNA synthetases (AARSs) are at the center of the question of the origin of life. They constitute a family of enzymes integrating the two levels of cellular organization: nucleic acids and proteins. AARSs arose early in evolution and are believed to be a group of ancient proteins. They are responsible for attaching amino acid residues to their cognate tRNA molecules, which is the firs...
متن کاملPredicting Mitochondrial tRNA Modification
M itochondria are integral to proper cell function, and mutations in its small genome (mtDNA) are associated with many diseases, along with the progression of normal aging [9]. While mtDNA has been extensively studied, not much is known about transcriptional variations of mitochondrial genes [3]. Recently, tRNA modifications have been the focus of intense study owing to their putative role in d...
متن کاملAminoacyl-tRNA synthetases database Y2K
The aminoacyl-tRNA synthetases (AARS) are a diverse group of enzymes that ensure the fidelity of transfer of genetic information from DNA into protein. They catalyse the attachment of amino acids to transfer RNAs and thereby establish the rules of the genetic code by virtue of matching the nucleotide triplet of the anticodon with its cognate amino acid. Currently, 818 AARS primary structures ha...
متن کاملIsolation of Saccharomyces cerevisiae mitochondrial formyltetrahydrofolic acid:methionyl-tRNA transformylase and the hybridization of mitochondrial fMet-tRNA with mitochondrial DNA.
Formyltetrahydrofolic acid:methionyl-tRNA transformylase was isolated from Saccharomyces cerevisiae mitochondria and used to prepare yeast mitochondrial [(3)H]formylmethionyl-tRNA. This fMet-tRNA hybridizes with mitochondrial DNA but not with yeast nuclear or E. coli DNA. Unlabeled mitochondrial, but not extramitochondrial, tRNA competes in this reaction. tRNA was eluted from the hybrid and fou...
متن کاملThe N-terminal domain of mammalian Lysyl-tRNA synthetase is a functional tRNA-binding domain.
Lysyl-tRNA synthetase from higher eukaryotes possesses a lysine-rich N-terminal polypeptide extension appended to a classical prokaryotic-like LysRS domain. Band shift analysis showed that this extra domain provides LysRS with nonspecific tRNA binding properties. A N-terminally truncated derivative of LysRS, LysRS-DeltaN, displayed a 100-fold lower apparent affinity for tRNA(3)Lys and a 3-fold ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: RNA
سال: 2007
ISSN: 1355-8382
DOI: 10.1261/rna.588407