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Nucleic Acids Research, 1980, Vol. 8, No. 16 3639-3658
© 1980

MOLECULAR BIOLOGY

The release of 40S hnRNP particles by brief digestion of HeLa nuclei with micrococcal nuclease

Barbara Webb Walker, Leonard Lothstein, C.Leslie Baker and Wallace M. LeStourgeon

Department of Molecular Biology, Vanderbilt University Nashville, TN 37235, USA

Received April 9, 1980. Brief digestion of HeLa nuclei with micrococcal nuclease releases monomer hnRNP particles as well as monomer and polynucleosomes. sucrose gradient analysis of the nuclease releaaed material reveals a series of small A260 peaks overlapping a more predominant peak in the 40S region of the gradient. Analysis of the proteins, DNA, and RNA in successive gradient fractions has confirmed that the smaller peaks are monomer and polynucleoaomes, and that the larger peak is 40S hnRNP. Like 40S particles isolated by low salt extraction or by sonication, the nuclease released particles are composed of rapidly labeled RNA associated with a group of non-histone proteins the most predominant of which are the 32,000–44,000 MW proteins previously identified as core hnRNP proteins. These results provide further evidence that 40S hnRNP particles exist as discrete structural components of larger in vivo ribonucleoprotein complexes.


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