Overexpression of DEAD Box Protein PMSS116 Promotes ATP-dependent Splicing of a Yeast Group II Intron in Vitro

Overview

Journal Nucleic Acids Res

Publisher Oxford University Press

Specialty Biochemistry

Date 1995 Aug 11

PMID 7659519

Citations 10

Authors

I Niemer

C Schmelzer

G V Borner

Affiliations

Soon will be listed here.

Abstract

The group II intron bI1, the first intron of the mitochondrial cytochrome b gene in yeast is self-splicing in vitro. Genetic evidence suggests that trans-acting factors are required for in vivo splicing of this intron. In accordance with these findings, we present in vitro data showing that splicing of bI1 under physiological conditions depends upon the presence of proteins of a mitochondrial lysate. ATP is an essential component is this reaction. Overexpression of the nuclear-encoded DEAD box protein pMSS-116 results in a marked increase in the ATP-dependent splicing activity of the extract, suggesting that pMSS116 may play an important role in splicing of bI1.

Citing Articles

The DEAD-box helicase Mss116 plays distinct roles in mitochondrial ribogenesis and mRNA-specific translation.

De Silva D, Poliquin S, Zeng R, Zamudio-Ochoa A, Marrero N, Perez-Martinez X Nucleic Acids Res. 2017; 45(11):6628-6643.

PMID: 28520979 PMC: 5499750. DOI: 10.1093/nar/gkx426.

Evolution of group II introns.

Zimmerly S, Semper C Mob DNA. 2015; 6:7.

PMID: 25960782 PMC: 4424553. DOI: 10.1186/s13100-015-0037-5.

Yeast DEAD box protein Mss116p is a transcription elongation factor that modulates the activity of mitochondrial RNA polymerase.

Markov D, Wojtas I, Tessitore K, Henderson S, McAllister W Mol Cell Biol. 2014; 34(13):2360-9.

PMID: 24732805 PMC: 4054322. DOI: 10.1128/MCB.00160-14.

ATP utilization and RNA conformational rearrangement by DEAD-box proteins.

Henn A, Bradley M, De La Cruz E Annu Rev Biophys. 2012; 41:247-67.

PMID: 22404686 PMC: 7761782. DOI: 10.1146/annurev-biophys-050511-102243.

Mechanism of Mss116 ATPase reveals functional diversity of DEAD-Box proteins.

Cao W, Coman M, Ding S, Henn A, Middleton E, Bradley M J Mol Biol. 2011; 409(3):399-414.

PMID: 21501623 PMC: 3125984. DOI: 10.1016/j.jmb.2011.04.004.

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