Literature DB >> 9223272

Association of the mammalian helicase MAH with the pre-mRNA splicing complex.

G M Molnar1, A Crozat, S K Kraeft, Q P Dou, L B Chen, A B Pardee.   

Abstract

Conversion of pre-mRNAs into mature mRNAs includes several consecutive enzymatic modification steps that are carried out in the spliceosomes. Helicases have been shown to contribute to these catalytic processes both in yeast and in mammalian cells. Our results identify the mammalian protein MAH (matrix-associated helicase) as a new helicase present in the spliceosome complex. Sequence comparison describes MAH as the first higher eukaryotic member of the helicase superfamily I, with demonstrated enzymatic activity. Because MAH does not bind small nuclear ribonucleoproteins (snRNPs), it appears to be a non-snRNP binding factor of the splicing complex. In conclusion, our data suggest the involvement of MAH in processing of pre-mRNAs in mammalian cells.

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Year:  1997        PMID: 9223272      PMCID: PMC21514          DOI: 10.1073/pnas.94.15.7831

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


  45 in total

1.  Requirement of the RNA helicase-like protein PRP22 for release of messenger RNA from spliceosomes.

Authors:  M Company; J Arenas; J Abelson
Journal:  Nature       Date:  1991-02-07       Impact factor: 49.962

2.  A mutational analysis of spliceosome assembly: evidence for splice site collaboration during spliceosome formation.

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Journal:  Genes Dev       Date:  1987-08       Impact factor: 11.361

3.  Molecular cloning of an enhancer binding protein: isolation by screening of an expression library with a recognition site DNA.

Authors:  H Singh; J H LeBowitz; A S Baldwin; P A Sharp
Journal:  Cell       Date:  1988-02-12       Impact factor: 41.582

4.  Stepwise assembly of a pre-mRNA splicing complex requires U-snRNPs and specific intron sequences.

Authors:  D Frendewey; W Keller
Journal:  Cell       Date:  1985-08       Impact factor: 41.582

5.  A multicomponent complex is involved in the splicing of messenger RNA precursors.

Authors:  P J Grabowski; S R Seiler; P A Sharp
Journal:  Cell       Date:  1985-08       Impact factor: 41.582

Review 6.  Non-snRNP protein splicing factors.

Authors:  G M Lamm; A I Lamond
Journal:  Biochim Biophys Acta       Date:  1993-06-25

7.  Messenger RNA splicing in vitro: an excised intervening sequence and a potential intermediate.

Authors:  P J Grabowski; R A Padgett; P A Sharp
Journal:  Cell       Date:  1984-06       Impact factor: 41.582

8.  Identification of a nuclear protein matrix.

Authors:  R Berezney; D S Coffey
Journal:  Biochem Biophys Res Commun       Date:  1974-10-23       Impact factor: 3.575

9.  A cold-sensitive mRNA splicing mutant is a member of the RNA helicase gene family.

Authors:  E J Strauss; C Guthrie
Journal:  Genes Dev       Date:  1991-04       Impact factor: 11.361

10.  Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase.

Authors:  K L Guan; J E Dixon
Journal:  Anal Biochem       Date:  1991-02-01       Impact factor: 3.365

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5.  Clinical diversity caused by novel IGHMBP2 variants.

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7.  DNA/RNA helicase gene mutations in a form of juvenile amyotrophic lateral sclerosis (ALS4).

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Review 8.  RNA processing defects associated with diseases of the motor neuron.

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9.  Transgenic rescue of neurogenic atrophy in the nmd mouse reveals a role for Ighmbp2 in dilated cardiomyopathy.

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10.  Truncating and missense mutations in IGHMBP2 cause Charcot-Marie Tooth disease type 2.

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