Histone H1-like, lysine-rich low complexity amino acid extensions in mosquito ribosomal proteins RpL23a and RpS6 have evolved independently.

Histone H1-like, lysine-rich low complexity amino acid extensions in mosquito ribosomal proteins RpL23a and RpS6 have evolved independently. Research Abstract Details 

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Histone H1-like, lysine-rich low complexity amino acid extensions in mosquito ribosomal proteins RpL23a and RpS6 have evolved independently. Abstract Text:

Vida P Hernandez,A M Fallon,

Histone H1-like amino acid extensions have been described at the amino terminus of Drosophila RpL22 and RpL23a, and at the carboxyl terminus of mosquito ribosomal protein RpS6. An in silico search suggested that RpL23a, but not RpL22, in Anopheles gambiae has an amino-terminal extension. Because low complexity amino acid extensions are not common on eukaryotic ribosomal proteins, and their functions are unknown, we cloned cDNAs encoding RpL23a from Aedes albopictus and Anopheles stephensi mosquito cell lines. RpL23a proteins in Aedes and Anopheles mosquitoes are rich in lysine (approximately 25%), alanine (approximately 21%), and proline (approximately 8%), have a mass of approximately 40 kDa, a pI of 11.4 to 11.5, and contain an N-terminal extension of approximately 260 amino acid residues. The N-terminal extension in mosquito RpL23a is about 100 amino acids longer than that in the Drosophila RpL23a homolog, and contains several repeated amino acid motifs. Analysis of exon-intron organization in the An. gambiae and in D. melanogaster genes suggests that a short first exon encodes a series of 11 amino acid residues conserved in RpL23a proteins from Drosophila, mosquitoes, and the moth, Bombyx mori. The histone H1-like sequence in RpL23a is encoded entirely within the second exon. The C-terminal 126 amino acid residues of the RpL23a protein, encoded by exon 3 in Drosophila, and by exons 3 and 4 in Anopheles gambiae, are well conserved, and correspond to Escherichia coli RpL23 with the addition of the eukaryotic N-terminal nuclear localization sequence. Sequence comparisons indicate that the histone H1-like extensions on mosquito RpS6 and RpL23a have evolved independently of each other, and of histone H1 proteins.

Histone H1-like, lysine-rich low complexity amino acid extensions in mosquito ribosomal proteins RpL23a and RpS6 have evolved independently. Publishing Authors By Initials

VP Hernandez,AM Fallon,

For similar investigative techniques: genetic techniques: sequence analysis: sequence analysis, dna research abstracts see: investigative techniques: genetic techniques: sequence analysis: sequence analysis, dna research

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Histone H1-like, lysine-rich low complexity amino acid extensions in mosquito ribosomal proteins RpL23a and RpS6 have evolved independently. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Archives of insect biochemistry and physiology

VOLUME: 64

Page Numbers: 100-10

Journal Abbreviation: Arch. Insect Biochem. Physiol.

ISSN: 0739-4462

DAY: 3

MONTH: Feb

YEAR: 2007

Histone H1-like, lysine-rich low complexity amino acid extensions in mosquito ribosomal proteins RpL23a and RpS6 have evolved independently. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 8501752

Histone H1-like, lysine-rich low complexity amino acid extensions in mosquito ribosomal proteins RpL23a and RpS6 have evolved independently. Keywords Mesh Terms:

KEYWORDS: Sequence Analysis, DNA

MESH TERMS: metabolism

Chemical & Substance for Abstract: Histone H1-like, lysine-rich low complexity amino acid extensions in mosquito ribosomal proteins RpL23a and RpS6 have evolved independently. Information

Substance Name: RNA

Registry Number: 63231-63-0

Grant and Affiliation Information for Histone H1-like, lysine-rich low complexity amino acid extensions in mosquito ribosomal proteins RpL23a and RpS6 have evolved independently.

AFFILIATION: Department of Entomology, University of Minnesota, St. Paul, MN 55108, USA.

Country: United States

AGENCY: United States NIAID

GRANT: AI20385

ACRONYM: AI

MEDLINETA: Arch Insect Biochem Physiol

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ACCESSION NUMBER: AY972826

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