Primary structure differences between proteins C1 and C2 of HeLa 40S nuclear ribonucleoprotein particles.

Abstract:

:Partial acid cleavage, comparative HPLC tryptic peptide mapping and amino acid sequencing of the C1 and C2 proteins of HeLa heterogeneous nuclear ribonucleoprotein (hnRNP) particles demonstrate that proteins C1 and C2 differ in primary structure by the presence of a 13 amino acid insert sequence in C2. This C2 insert sequence occurs after either glycine 106 or serine 107 in C1. The additional 13 amino acids that are present in C2 account for the observed molecular weight difference between the C1 and C2 hnRNP proteins on SDS polyacrylamide gel electrophoresis. Because C1 and C2 appear identical except for the 13 residue insert and because the 3' and 5' untranslated regions of the corresponding mRNAs also appear to be the same (Swanson et al., Mol. Cell. Biol. 7: 1731-1739), it is possible that both polypeptides are produced from a single transcription unit through an alternative splicing mechanism.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Merrill BM,Barnett SF,LeStourgeon WM,Williams KR

doi

10.1093/nar/17.21.8441

subject

Has Abstract

pub_date

1989-11-11 00:00:00

pages

8441-9

issue

21

eissn

0305-1048

issn

1362-4962

journal_volume

17

pub_type

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