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Alternative processing of mRNAs encoding mammalian chromosomal high-mobility-group proteins HMG-I and HMG-Y

K R Johnson1, D A Lehn, R Reeves

  • 1Program in Genetics and Cell Biology Washington State University, Pullman 99164.

Insights

High-mobility-group protein HMG-I and its isoform HMG-Y arise from alternative RNA processing of a single gene. This explains sequence variations found in cDNA clones from human cells.

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • High-mobility-group protein HMG-I is a nonhistone chromosomal protein.
  • HMG-I is expressed in rapidly dividing cells and binds A.T-rich DNA regions.
  • HMG-I localizes to specific regions of mammalian metaphase chromosomes.

Purpose of the Study:

  • To investigate the molecular basis of HMG-I and HMG-Y isoforms.
  • To analyze sequence variations in cDNA clones encoding HMG-I and HMG-Y.
  • To determine the origin of HMG-I/HMG-Y heterogeneity.

Main Methods:

  • Isolation of eight cDNA clones encoding HMG-I and HMG-Y from a human Raji cell library.
  • Analysis of nucleotide sequence rearrangements in 5'-untranslated regions.
  • Identification of in-frame deletions in the open reading frame (ORF).
  • Sequencing of a human HMG-I/HMG-Y retropseudogene.

Main Results:

  • Nucleotide sequence rearrangements were detected in the 5'-untranslated regions of cDNA clones.
  • Five of eight cDNA clones exhibited 33- or 36-base-pair in-frame deletions in the ORF, encoding HMG-Y.
  • Evidence suggests alternative RNA processing from a single functional gene generates HMG-I and HMG-Y isoforms.
  • A processed HMG-Y retropseudogene was identified in the human genome.

Conclusions:

  • HMG-I and HMG-Y protein isoforms result from alternative RNA processing of a single gene.
  • Sequence heterogeneity in cDNA clones is attributed to alternative splicing and processing.
  • The human genome contains multiple, likely nonfunctional, HMG-I/HMG-Y gene copies.

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