PMID- 10079173
OWN - NLM
STAT- MEDLINE
DCOM- 19990413
LR  - 20151119
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 256
IP  - 2
DP  - 1999 Mar 16
TI  - Analysis of the RNA recognition motifs of human neuronal ELAV-like proteins in
      binding to a cytokine mRNA.
PG  - 263-8
AB  - Human neuronal Elav-like proteins contain three RNP-type RNA recognition motifs
      (RRMs). Previous reports demonstrated that a single RRM of the proteins is not
      sufficient to bind to the uridine-rich stretch in the 3' untranslated region of
      mRNAs and that the bi-RRM peptide consisting of the first two RRMs is necessary
      for the binding. The present study was designed to examine the potential
      contributions of the first two RRMs when binding to a cytokine mRNA. Deletions of
      the internal or terminal amino acid residues of the first RRM (RRM1) of the
      HuC/ple21 ELAV-like protein completely abolished RNA binding. However, removal of
      any region of the second RRM (RRM2) except for the eight amino acid residues,
      which correspond to the potent fourth beta-sheet structure of RRM2, did not
      affect RNA binding. Conjugation of the eight amino acid residues to RRM1 enhanced
      the RNA binding as well as the entire RRM2, indicating that the octapeptide of
      RRM2 can be compensated for by the binding function of RRM2. The present study
      also showed that the substitutions of glutamic acid at 42 for aspartic acid and
      leucine at 44 for phenylalanine in the first potent alpha-helix structure of
      RRM1, as were seen in another ELAV-like protein Hel-N1, markedly affected the RNA
      binding.
CI  - Copyright 1999 Academic Press.
FAU - Sakai, K
AU  - Sakai K
AD  - Department of Neurology, Kanazawa Medical University, 1-1 Daigaku,
      Uchinada-machi, Ishikawa, Kahoku-gun, 920-02, Japan.
FAU - Kitagawa, Y
AU  - Kitagawa Y
FAU - Hirose, G
AU  - Hirose G
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (3' Untranslated Regions)
RN  - 0 (ELAV Proteins)
RN  - 0 (ELAV-Like Protein 2)
RN  - 0 (ELAVL2 protein, human)
RN  - 0 (Interleukin-3)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Peptide Fragments)
RN  - 0 (RNA, Messenger)
RN  - 0 (RNA-Binding Proteins)
SB  - IM
MH  - 3' Untranslated Regions/genetics
MH  - Amino Acid Sequence
MH  - Amino Acid Substitution
MH  - Binding Sites
MH  - ELAV Proteins
MH  - ELAV-Like Protein 2
MH  - Humans
MH  - Interleukin-3/*genetics
MH  - Molecular Sequence Data
MH  - Nerve Tissue Proteins/*chemistry/genetics/*metabolism
MH  - Peptide Fragments/chemistry/metabolism
MH  - Protein Structure, Secondary
MH  - RNA, Messenger/*metabolism
MH  - RNA-Binding Proteins/*chemistry/genetics/*metabolism
MH  - Sequence Alignment
MH  - Sequence Deletion/genetics
EDAT- 1999/03/18 00:00
MHDA- 1999/03/18 00:01
CRDT- 1999/03/18 00:00
PHST- 1999/03/18 00:00 [pubmed]
PHST- 1999/03/18 00:01 [medline]
PHST- 1999/03/18 00:00 [entrez]
AID - S0006-291X(99)90282-6 [pii]
AID - 10.1006/bbrc.1999.0282 [doi]
PST - ppublish
SO  - Biochem Biophys Res Commun. 1999 Mar 16;256(2):263-8. doi:
      10.1006/bbrc.1999.0282.