Distribution of B52 Within a Chromosomal Locus Depends on the Level of Transcription

Overview

Journal Mol Biol Cell

Specialties Cell Biology
Molecular Biology

Date 1994 Jan 1

PMID 8186467

Citations 6

Authors

D T Champlin

J T Lis

Affiliations

Soon will be listed here.

Abstract

Drosophila B52 protein is a homologue of human ASF/SF2 that functions in vitro as an essential pre-mRNA splicing factor. Immunofluorescence analysis of polytene chromosomes has shown that B52 generally colocalizes with RNA polymerase II; however, in contrast to other splicing factors, B52 brackets RNA polymerase II at highly active heat-shock puffs. Also, UV cross-linking in nonpolytene cells has shown that B52 cross-links in vivo to DNA flanking the highly active transcription units. Here, we find that the distribution of cross-linked B52 at heat-shock loci depends on transcription levels. Heat shocks at low and moderate temperatures, which induce corresponding levels of transcription, recruit B52 both to transcribed DNA and to flanking DNA, whereas a full heat-shock induction concentrates B52 on the DNA that brackets the entire activated region. We have also identified a 46-kDa protein from Chironomus tentans that binds Drosophila B52 antibodies and has a distribution on chromosomes analogous to B52. This protein is found throughout the moderately transcribed Balbiani rings. However, when transcription at these rings is hyperinduced to levels comparable to fully induced Drosophila heat-shock genes, the protein is restricted to the boundaries of highly decondensed chromatin. We suggest that B52 tracks to chromatin fibers that are folding or unfolding, and we discuss this in light of B52's proposed roles in pre-mRNA splicing and control.

Citing Articles

The splicing factor SC35 has an active role in transcriptional elongation.

Lin S, Coutinho-Mansfield G, Wang D, Pandit S, Fu X Nat Struct Mol Biol. 2008; 15(8):819-26.

PMID: 18641664 PMC: 2574591. DOI: 10.1038/nsmb.1461.

Nuclear history of a pre-mRNA determines the translational activity of cytoplasmic mRNA.

Matsumoto K, Wassarman K, Wolffe A EMBO J. 1998; 17(7):2107-21.

PMID: 9524132 PMC: 1170555. DOI: 10.1093/emboj/17.7.2107.

The intracisternal A-particle proximal enhancer-binding protein activates transcription and is identical to the RNA- and DNA-binding protein p54nrb/NonO.

Basu A, Dong B, Krainer A, HOWE C Mol Cell Biol. 1997; 17(2):677-86.

PMID: 9001221 PMC: 231793. DOI: 10.1128/MCB.17.2.677.

Altered levels of the Drosophila HRB87F/hrp36 hnRNP protein have limited effects on alternative splicing in vivo.

Zu K, Sikes M, Haynes S, Beyer A Mol Biol Cell. 1996; 7(7):1059-73.

PMID: 8862520 PMC: 275958. DOI: 10.1091/mbc.7.7.1059.

CHD1 is concentrated in interbands and puffed regions of Drosophila polytene chromosomes.

Stokes D, Tartof K, PERRY R Proc Natl Acad Sci U S A. 1996; 93(14):7137-42.

PMID: 8692958 PMC: 38949. DOI: 10.1073/pnas.93.14.7137.

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